People

Dr Mike Hough

Senior Lecturer
School of Biological Sciences
Dr Mike Hough
  • Email

  • Telephone

    +44 (0) 1206 873317

  • Location

    3SW.5.15B, Colchester Campus

Profile

Biography

BSc (Hons) Physics 1995 PhD Structural Biology 1999 Fellow of the Higher Education Academy (FHEA) Fellow of the Royal Society of Biology (FRSB) Member of the Royal Society of Chemistry (MRSC) and Member of the Institute of Physics (MInstP) Member of the Biochemical Society, the British Crystallographic Association and the Inorganic Biochemistry Discussion Group of the RSC. My Google Scholar page is: https://scholar.google.co.uk/citations?user=OCfvOG0AAAAJ ORCID http://orcid.org/0000-0001-7377-6713 Research Gate: https://www.researchgate.net/profile/Michael_Hough2 Twitter: https://twitter.com/mikehough73 Interested in joining us? I am always happy to discuss opportunities with students with self-arranged funding, or with students or postdoctoral fellows interested in fellowship opportunities that match our research interests. Masters (by research) projects are available on a self-funded basis in all of the research areas described on this page. Typical Home/EU fees are £4200 for a 1 year programme, with an additional-project dependent bench fee. Please contact me at any time to discuss the possibilities to work with us in this way. Marie Curie Fellowships The EU operates the Marie Curie Individual fellowship scheme to promote mobility of Early Career researchers. Fellowship applications are welcome in any of the areas of research described here. Applications are particularly welcome in: (i) Haem protein structural biology, particularly gas-sensor proteins (ii) Advanced X-ray methods development including single crystal spectroscopy and radiolysis (iii) Microbial biotechnology, to compement our existing programmes on napthenic acid biodegradation and isoprene sythesis/degradation (iv) Electron and protein transfer mechanisms in metalloproteins The scheme supports two year fellowships to move from one EU member country to another, with the stipulation a) that there is no previous strong association of the person to new host country, in terms of having worked there in the recent past b) that the person either has a PhD, or has four years postgraduate research experience at the point of application. Note, you do not have to be an EU citizen to benefit from this scheme - what is required is that you currently reside in the EU. Research in my group seeks to understand the relationship between protein function, structure and dynamics, with a particular focus on metal-containing enzymes, enzymes in biotechnology and heme sensor proteins. We work in close collaboration with scientists at synchrotron radiation facilities in the field of structural biology method development. From left: Preye Odubo, Demet Kekilli, Hannah Adams, Mike Hough, Tadeo Moreno Chicano, Sam Horrell, Karl Skeels Current Group Members Tadeo Moreno Chicano: PhD student - Enzyme Catalysis in Action: 3D Movies of X-ray Induced Chemical Reactions in protein Crystals - funded by the Leverhulme Trust Preye Odubo: PhD student (jointly supervised with Dr McGenity) - Finding New Diversities of Isoprene Synthases in Bacteria Karl Skeels: BBSRC CASE PhD student (jointly supervised with Dr Whitby) - Using synthetic biology to forward engineer napthenic acid catabolic pathways in Pseudomonads for use as biotechnological tools in NA biormediation - funded by BBSRC Hannah Adams: PhD student (part time) Structure and function of cytochrome c' from Methylococcus capsulatus Bath. Ali Ebrahim: PhD student - 'Methods and Instrumentation for Collection and Validation of Damage-Free Protein Structures in Defined Redox States. - Joint Essex / Diamond Light Source studentship. Former group members Dr Demet Kekilli:Postdoctoral researcher - Enzyme Catalysis in Action: 3D Movies of X-ray Induced Chemical Reactions in protein Crystals - funded by the Leverhulme Trust - Demet moved to a PSI-FELLOW position the Paul Scherrer Institute, Switzerland in May 2017. Dr Sam Horrell: Postdoctoral researcher - Dynamics of Electron and Proton Transfer Chemistry in Copper and Hybrid Copper-Haem Enzymes - funded by BBSRC - Sam moved to the University of Hamburg / DESY, Germany in April 2017. Our major research themes include: Development and application (in collaboration with scientists at synchrotron facilities) of single crystal optical, resonance Raman and X-ray absorption (XAFS) methodologies as tools to fingerprint redox and ligand states in metalloprotein crystals during crystallography experiments. Using X-rays to drive redox reactions in crystals in collaboration withDiamond Light Source and the Swiss Light Source. We recently published an article in this area in the IUCr Journal, with a supporting commentary. Structural and functional studies of the gas sensing cytochromes c'and their fascinating ability to distinguish between the small gaseous ligands NO and CO by binding them to opposite faces of haem while avoiding oxygen binding. Catalytic mechanism of enzymes from the bacterial denitrification pathway, principally Cu-containing nitrite reductase (NiR) which catalyses the reduction of nitrite to NO. This work involves a close collaboration withDr Richard Strange at Essex and Drs Tom Keal and Chin Yong at STFC Hartree Centre. More broadly, this work is conducted in collaboration with the group of Professor Samar Hasnain at the University of Liverpool who have a parallel experimental research project on three domain CuNiR. In collaboration with DrJonathan Worrall, studies ofCu trafficking and homeostasis in Streptomycetes. Environmental enzymology studies of napthenic acid metabolism in oil sands wastewaters (collaboration with Dr Corinne Whitby) and isoprene production(collaboration with Dr Terry McGenity). Development of in vivo biosensors for use in plants (collaboration with Prof Phil Mullineaux, Dr Richard Strange, Dr Phillipe Laissue and Dr Greg Brooke). New sample delivery methods to study microcrystals in chip fixed targets (with Dr Robin Owen) and using microfluidic based rapid mixing for time-resolved crystallography (with Dr Diana Monteiro and Prof Martin Trebbin, Center for Ultrafast Imaging, University of Hamburg). Research environment and life in our group We are based in a well-equipped structural biology laboratory (lab 5.08) in the School of Biological Sciences together with the groups of Jonathan Worrall and Filippo Prischi. Group members make extensive useof state of the art national and international facilities to which we have access, including Diamond Light Source, Swiss Light Source and the European Synchrotron Radiation Facility in Grenoble. We have several external collaborations that provide additional opportunities to group members. Our research is supported by funding awards from the BBSRC and Leverhulme Trust. Swiss Light Source beamtime. From left - Florian Dworkowski, Mike Hough, Tadeo Chicano, Demet Kekilli Diamond Light Source, the UK's facility for synchrotron radiation Current external collaborations DrFlorian Dworkowski(Swiss Light Source) - Single crystal spectroscopy of heme and Cu proteins DrRobin Owen(Diamond Light Source) - Damage-free structures through rapid data collection ProfessorColin Andrew, University of Eastern Oregon - Cytochrome c prime, kinetics and resonance Raman studies TheMolecular Biophysics Group(Dr Svetlana Antonyuk & Professors Robert R. Eady and S. Samar Hasnain) at the University of Liverpool: Catalysis in crystals, denitrification enzymes ProfessorNigel Scrutton'sgroup at the Manchester Institute of Biotechnology and the Harwell Research Complex: ultrafast kinetics (transient absorption and transient infrared spectroscopies) analysis of metalloproteins Dr Reza Ghiladi, North Carolina State University: Structure and mechanism of dehaloperoxidase enzymes Dr Diana Monteiro and Prof Martin Trebbin at CUI, University of Hamburg/DESY: Microfluiding mixing for time-resolved crystallography. As part of our comittment to research-led teaching, my lab hosts undergraduate students for summer placements. Previous placement students have been externally funded by the Wellcome Trust and the Biochemical Society as well as placements under the University's UROP scheme. Wellcome Trust Vacation Studentship holders Gemma Newton and Emily Colley - in the lab with Mike and Jonathan Worrall.

Qualifications

  • PhD Structural Biology Daresbury Laboratory and De Montfort University,

Research and professional activities

Research interests

Serial crystallography using XFEL and synchrotron radiation

We use the latest X-ray free electron laser (XFEL) facilities including SACLA in Japan to produce crystal structures of metalloproteins without the effects of radiation damage that can compromise interpretation of structures determined by conventional synchrotron X-ray crystallography. We particularly apply this method to high valent states of Fe and Cu proteins relevant to enzyme mechanisms.

Key words: crystallography
Open to supervise

X-ray crystallography of Metalloproteins

We determine high resolution X-ray crystal structures of metalloproteins to establish their functional mechanisms. We combine this with single crystal spectroscopy of the crystals to validate redox and ligand states in the structures.

Key words: Structural Biology
Open to supervise

MSOX Crystallography

We are developing a new method to determine sequences of crystal structures of metalloproteins, where the X-rays used to determine structures are also used to drive redox reactions within those crystals to access catalytic intermediate states. This is combined with advanced computational simulation of the enzymes (quantum mechanics and molecular dynamics) and single crystal spectroscopies to fully characterise such mechanisms.

Key words: Crystallography, metalloproteins
Open to supervise

Cytochromes and Gas Sensors

We are characterising the interaction of nitric oxide and carbon monoxide to cytochromes c', proteins which are analogous to mammalian gas sensors involved in vasodilation. This work combines structural biology, kinetics and spectroscopy.

Open to supervise

Development of in vivo biosensors for use in plants

Engineering of advanced in vivo biosensors (collaboration with Prof Phil Mullineaux, Dr Richard Strange, Dr Phillipe Laissue and Dr Greg Brooke).

Key words: Biosensors
Open to supervise

Environmental enzymology studies of napthenic acid metabolism in oil sands wastewaters (collaboration with Dr Corinne Whitby)

Key words: Bioremediation
Open to supervise

Development of genetic probes based on GFP for non-invasive detection and quantification of reactive oxygen species and antioxidants in subcellular compartments

Fluorescent protein biosensors are showing great promise in allowing the real time, spatial and quantitative detection of specific small molecules in living cells. We have engineered and used these biosensors in cells of the leaf to detect hydrogen peroxide, glutathione, lipid peroxides, oxidised ascorbate (vitamin C) and changes in pH. The detection spatially in real time has allowed us to develop a new hypothesis on the spatial dependency of signalling from chloroplasts to the nucleus in leaves exposed to high light - only those chloroplast in contact with the nucleus are capable of triggering a change in gene expression in response to high light. We have provided evidence, using these biosensors, that hydrogen peroxide is the mobile signal that transfers directly to the nucleus from connected chloroplasts. This work has led to further developments in biosensor technology in my laboratory, which in collaboration with colleagues in the School is beginning to extend our detection capability to animals cells and for studying other important signalling molecules.

Key words: green fluorescent protein

Methanotrophic cytochromes and their role in the nitrogen cycle

Structural biology and Biochemistry of cytochromes P460 and cytochromes c prime -beta from methanotrophic microorganisms

Open to supervise

Conferences and presentations

Fixed Target Serial Crystallography at Synchrotron and XFEL beamlines

Invited presentation, Diamond MX User Meeting 2019, East Midlands Conference Centre, 8/1/2019

Serial Crystallography (pump-n-probe)

Invited presentation, Diamond-II Workshop, Diamond Light Source, 10/9/2018

Time and sample efficient fixed targetserial crystallography ofmetalloenzymes using XFEL andsynchrotron beamlines

Invited presentation, MRC-KHIDI UK-Korea Research Symposium, Diamond Light Source, Harwell Campus, 16/8/2018

Many Structures from One Crystal (MSOX): A versatile approach to characterising redox enzyme reactions in protein crystals

Invited presentation, CCP4 Study Weekend 2018, East Midlands Conference Centre, Nottingham, United Kingdom, 11/1/2018

12th International Conference on Biology and Synchrotron Radiation, Stanford, USA, 21-24th August 2016

2016

30th European Crystallographic Meeting, Basel, Switzerland, 28 August-1 September 2016.

2016

9th International Meeting on X-ray Damage to Biological Crystalline Samples, Lund, Sweden, 9-11th March 2016.

The British Biophysical Society biennial meeting New horizons and emerging biomedical challenges for biophysics, July 6-8th Liverpool

Work on the ENCATS project was presented to the public at Daresbury Laboratorys Open week on 7-9th July.

Teaching and supervision

Current teaching responsibilities

  • Quantitative methods for Life Sciences (BS141)

  • Biomedical Science: Practice and Employability (BS214)

  • Metals in Biology (BS228)

  • Proteins and Macromolecular Assemblies (BS230)

  • Mechanisms of Neurological Disease (BS350)

  • Research Project in Biomolecular Science (BS831)

Previous supervision

Tadeo Moreno Chicano
Tadeo Moreno Chicano
Thesis title: Structural Characterisation of Ligand, Redox and Catalytic States in Haem Enzymes Using in Crystallo Spectroscopies and Serial Crystallography.
Degree subject: Biological Sciences
Degree type: Doctor of Philosophy
Awarded date: 23/4/2019
Demet Kekilli
Demet Kekilli
Thesis title: Ligand Discrimination Mechanisms in Cytochromes C Prime
Degree subject: Biochemistry
Degree type: Doctor of Philosophy
Awarded date: 24/6/2015

Publications

Journal articles (58)

Ebrahim, A., Appleby, MV., Axford, D., Beale, J., Moreno-Chicano, T., Sherrell, DA., Strange, RW., Hough, MA. and Owen, RL., (2019). Resolving polymorphs and radiation-driven effects in microcrystals using fixed-target serial synchrotron crystallography. Acta Crystallographica Section D Structural Biology. 75 (2), 151-159

Adams, HR., Krewson, C., Vardanega, JE., Fujii, S., Moreno-Chicano, T., Sambongi, Y., Svistunenko, D., Paps, J., Andrew, CR. and Hough, MA., (2019). One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath). Chemical Science. 10 (10), 3031-3041

Chaplin, AK., Chicano, TM., Hampshire, BV., Wilson, MT., Hough, MA., Svistunenko, DA. and Worrall, JAR., (2019). An Aromatic Dyad Motif in Dye Decolourising Peroxidases Has Implications for Free Radical Formation and Catalysis. Chemistry – A European Journal

Straw, ML., Chaplin, AK., Hough, MA., Paps, J., Bavro, VN., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2018). A cytosolic copper storage protein provides a second level of copper tolerance in Streptomyces lividans.. Metallomics : integrated biometal science. 10 (1), 180-193

Hough, MA. and Wilson, KS., (2018). From crystal to structure with CCP4. Acta Crystallographica. Section d, Structural Biology. 74 (2), 67-67

Horrell, S., Kekilli, D., Sen, K., Owen, RU., Dworkowski, FSN., Antonyuk, SV., Keal, TW., Yong, CW., Eady, RR., Hasnain, SS., Strange, RW. and Hough, MA., (2018). Enzyme catalysis captured using multiple structures from one crystal at varying temperatures. IUCrJ. 5 (3), 283-292

Sen, K., Hough, M., Strange, R., Yong, C. and Keal, T., (2018). A QM/MM Study of Nitrite Binding Modes in a Three-Domain Heme-Cu Nitrite Reductase. Molecules. 23 (11), 2997-2997

Kekilli, D., Petersen, CA., Pixton, DA., Ghafoor, DD., Abdullah, GH., Dworkowski, FSN., Wilson, MT., Heyes, DJ., Hardman, SJO., Murphy, LM., Strange, RW., Scrutton, NS., Andrew, CR. and Hough, MA., (2017). Engineering proximal vs. distal heme–NO coordination via dinitrosyl dynamics: implications for NO sensor design. Chemical Science. 8 (3), 1986-1994

Hough, MA., (2017). Choosing the optimal spectroscopic toolkit to understand protein function. Bioscience Reports. 37 (3), BSR20160378-BSR20160378

Kekilli, D., Moreno-Chicano, T., Chaplin, AK., Horrell, S., Dworkowski, FSN., Worrall, JAR., Strange, RW. and Hough, MA., (2017). Photoreduction and validation of haem?ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction. IUCrJ. 4 (3), 263-270

McCombs, NL., Moreno-Chicano, T., Carey, LM., Franzen, S., Hough, MA. and Ghiladi, RA., (2017). Interaction of Azole-Based Environmental Pollutants with the Coelomic Hemoglobin from Amphitrite ornata: A Molecular Basis for Toxicity. Biochemistry. 56 (17), 2294-2303

Chaplin, AK., Svistunenko, DA., Hough, MA., Wilson, MT., Vijgenboom, E. and Worrall, JAR., (2017). Active site maturation and activity of the copper-radical oxidase GlxA is governed by a tryptophan residue. The Biochemical Journal. 474 (5), 809-825

Sen, K., Horrell, S., Kekilli, D., Yong, CW., Keal, TW., Atakisi, H., Moreau, DW., Thorne, RE., Hough, MA. and Strange, RW., (2017). Active-site protein dynamics and solvent accessibility in native Achromobacter cycloclastes copper nitrite reductase. IUCrJ. 4 (4), 495-505

Horrell, S., Kekilli, D., Strange, RW. and Hough, MA., (2017). Recent structural insights into the function of copper nitrite reductases.. Metallomics. 9 (11), 1470-1482

Nilsson, ZN., Mandella, BL., Sen, K., Kekilli, D., Hough, MA., Moënne-Loccoz, P., Strange, RW. and Andrew, CR., (2017). Distinguishing Nitro vs Nitrito Coordination in Cytochrome c' Using Vibrational Spectroscopy and Density Functional Theory.. Inorganic Chemistry. 56 (21), 13205-13213

Deacon, OM., Karsisiotis, AI., Moreno-Chicano, T., Hough, MA., Macdonald, C., Blumenschein, TMA., Wilson, MT., Moore, GR. and Worrall, JAR., (2017). Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity.. Biochemistry. 56 (46), 6111-6124

Horrell, S., Antonyuk, SV., Eady, RR., Hasnain, SS., Hough, MA. and Strange, RW., (2016). Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal. IUCrJ. 3 (4), 271-281

Chaplin, AK., Wilson, MT., Hough, MA., Svistunenko, DA., Hemsworth, GR., Walton, PH., Vijgenboom, E. and Worrall, JAR., (2016). Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases. Journal of Biological Chemistry. 291 (24), 12838-12850

Porto, TV., Hough, MA. and Worrall, JAR., (2015). Structural insights into conformational switching in the copper metalloregulator CsoR fromStreptomyces lividans. Acta Crystallographica Section D Biological Crystallography. 71 (9), 1872-1878

Ghafoor, DD., Kekilli, D., Abdullah, GH., Dworkowski, FSN., Hassan, HG., Wilson, MT., Strange, RW. and Hough, MA., (2015). Hydrogen bonding of the dissociated histidine ligand is not required for formation of a proximal NO adduct in cytochrome c’. JBIC Journal of Biological Inorganic Chemistry. 20 (6), 949-956

Manole, A., Kekilli, D., Svistunenko, DA., Wilson, MT., Dobbin, PS. and Hough, MA., (2015). Conformational control of the binding of diatomic gases to cytochrome c′. JBIC Journal of Biological Inorganic Chemistry. 20 (4), 675-686

Servid, AE., McKay, AL., Davis, CA., Garton, EM., Manole, A., Dobbin, PS., Hough, MA. and Andrew, CR., (2015). Resonance Raman Spectra of Five-Coordinate Heme-Nitrosyl Cytochromes c′: Effect of the Proximal Heme-NO Environment. Biochemistry. 54 (21), 3320-3327

Chaplin, AK., Petrus, MLC., Mangiameli, G., Hough, MA., Svistunenko, DA., Nicholls, P., Claessen, D., Vijgenboom, E. and Worrall, JAR., (2015). GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis ofStreptomyces lividans. Biochemical Journal. 469 (3), 433-444

Brooke, GN., Gamble, SC., Hough, MA., Begum, S., Dart, DA., Odontiadis, M., Powell, SM., Fioretti, FM., Bryan, RA., Waxman, J., Wait, R. and Bevan, CL., (2015). Antiandrogens Act as Selective Androgen Receptor Modulators at the Proteome Level in Prostate Cancer Cells. Molecular & Cellular Proteomics. 14 (5), 1201-1216

Hough, MA. and Andrew, CR., (2015). Cytochromes c′. RECENT ADVANCES IN MICROBIAL OXYGEN-BINDING PROTEINS. 67, 1-84

Dworkowski, FSN., Hough, MA., Pompidor, G. and Fuchs, MR., (2015). Challenges and solutions for the analysis ofin situ,in crystallomicro-spectrophotometric data. Acta Crystallographica Section D Biological Crystallography. 71 (1), 27-35

Reeder, BJ. and Hough, MA., (2014). The structure of a class 3 nonsymbiotic plant haemoglobin fromArabidopsis thalianareveals a novel N-terminal helical extension. Acta Crystallographica Section D Biological Crystallography. 70 (5), 1411-1418

Barrier, E., Braz Fernandes, FM., Bujan, M., Feiters, MC., Froideval, A., Ghijsen, J., Hase, T., Hough, MA., Jergel, M., Jimenez, I., Kajander, T., Kikas, A., Kokkinidis, M., Kover, L., Larsen, HB., Lawson, DM., Lawniczak-Jablonska, K., Mariani, C., Mikulik, P., Monnier, J., Morera, S., McGuinness, C., Müller-Buschbaum, P., Meedom Nielson, M., Pietsch, U., Tromp, M., Simon, M., Stangl, J. and Zanotti, G., (2014). The benefit of the European User Community from transnational access to national radiation facilities. Journal of Synchrotron Radiation. 21 (3), 638-639

Blundell, KLIM., Hough, MA., Vijgenboom, E. and Worrall, JAR., (2014). Structural and mechanistic insights into an extracytoplasmic copper trafficking pathway inStreptomyces lividans. Biochemical Journal. 459 (3), 525-538

Kekilli, D., Dworkowski, FSN., Pompidor, G., Fuchs, MR., Andrew, CR., Antonyuk, S., Strange, RW., Eady, RR., Hasnain, SS. and Hough, MA., (2014). Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy. Acta Crystallographica Section D Biological Crystallography. 70 (5), 1289-1296

Hough, MA., Silkstone, G., Worrall, JAR. and Wilson, MT., (2014). NO Binding to the Proapoptotic Cytochrome c–Cardiolipin Complex. NITRIC OXIDE. 96, 193-209

Rajagopal, BS., Edzuma, AN., Hough, MA., Blundell, KLIM., Kagan, VE., Kapralov, AA., Fraser, LA., Butt, JN., Silkstone, GG., Wilson, MT., Svistunenko, DA. and Worrall, JAR., (2013). The hydrogen-peroxide-induced radical behaviour in human cytochromec–phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant. Biochemical Journal. 456 (3), 441-452

Russell, HJ., Hardman, SJO., Heyes, DJ., Hough, MA., Greetham, GM., Towrie, M., Hay, S. and Scrutton, NS., (2013). Modulation of ligand-heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond-second temporal range. FEBS Journal. 280 (23), 6070-6082

Doutch, J., Hough, MA., Hasnain, SS. and Strange, RW., (2012). Challenges of sulfur SAD phasing as a routine method in macromolecular crystallography. Journal of Synchrotron Radiation. 19 (1), 19-29

Dwarakanath, S., Chaplin, AK., Hough, MA., Rigali, S., Vijgenboom, E. and Worrall, JAR., (2012). Response to Copper Stress in Streptomyces lividans Extends beyond Genes under Direct Control of a Copper-sensitive Operon Repressor Protein (CsoR). Journal of Biological Chemistry. 287 (21), 17833-17847

Strange, RW., Hough, MA., Antonyuk, SV. and Hasnain, SS., (2012). Structural Evidence for a Copper-Bound Carbonate Intermediate in the Peroxidase and Dismutase Activities of Superoxide Dismutase. PLoS ONE. 7 (9), e44811-e44811

Antonyuk, SV. and Hough, MA., (2011). Monitoring and validating active site redox states in protein crystals. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1814 (6), 778-784

Leferink, NGH., Han, C., Antonyuk, SV., Heyes, DJ., Rigby, SEJ., Hough, MA., Eady, RR., Scrutton, NS. and Hasnain, SS., (2011). Proton-Coupled Electron Transfer in the Catalytic Cycle ofAlcaligenes xylosoxidansCopper-Dependent Nitrite Reductase. Biochemistry. 50 (19), 4121-4131

Hough, MA., Antonyuk, SV., Barbieri, S., Rustage, N., McKay, AL., Servid, AE., Eady, RR., Andrew, CR. and Hasnain, SS., (2011). Distal-to-Proximal NO Conversion in Hemoproteins: The Role of the Proximal Pocket. Journal of Molecular Biology. 405 (2), 395-409

Brenner, S., Heyes, DJ., Hay, S., Hough, MA., Eady, RR., Hasnain, SS. and Scrutton, NS., (2009). Demonstration of Proton-coupled Electron Transfer in the Copper-containing Nitrite Reductases. Journal of Biological Chemistry. 284 (38), 25973-25983

Hough, MA., Eady, RR. and Hasnain, SS., (2008). Identification of the Proton Channel to the Active Site Type 2 Cu Center of Nitrite Reductase: Structural and Enzymatic Properties of the His254Phe and Asn90Ser Mutants†,‡. Biochemistry. 47 (51), 13547-13553

Ellis, MJ., Buffey, SG., Hough, MA. and Hasnain, SS., (2008). On-line optical and X-ray spectroscopies with crystallography: an integrated approach for determining metalloprotein structures in functionally well defined states. Journal of Synchrotron Radiation. 15 (5), 433-439

Hough, MA., Antonyuk, SV., Strange, RW., Eady, RR. and Hasnain, SS., (2008). Crystallography with Online Optical and X-ray Absorption Spectroscopies Demonstrates an Ordered Mechanism in Copper Nitrite Reductase. Journal of Molecular Biology. 378 (2), 353-361

Paraskevopoulos, K., Hough, MA., Sawers, RG., Eady, RR. and Hasnain, SS., (2007). The structure of the Met144Leu mutant of copper nitrite reductase from Alcaligenes xylosoxidans provides the first glimpse of a protein–protein complex with azurin II. JBIC Journal of Biological Inorganic Chemistry. 12 (6), 789-796

Barrett, ML., Harvey, I., Sundararajan, M., Surendran, R., Hall, JF., Ellis, MJ., Hough, MA., Strange, RW., Hillier, IH. and Hasnain, SS., (2006). Atomic Resolution Crystal Structures, EXAFS, and Quantum Chemical Studies of Rusticyanin and Its Two Mutants Provide Insight into Its Unusual Properties†,‡. Biochemistry. 45 (9), 2927-2939

Strange, RW., Antonyuk, SV., Hough, MA., Doucette, PA., Valentine, JS. and Hasnain, SS., (2006). Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu–Zn, Zn–Zn and As-isolated Wild-type Enzymes. Journal of Molecular Biology. 356 (5), 1152-1162

Paraskevopoulos, K., Sundararajan, M., Surendran, R., Hough, MA., Eady, RR., Hillier, IH. and Hasnain, SS., (2006). Active site structures and the redox properties of blue copper proteins: atomic resolution structure of azurin II and electronic structure calculations of azurin, plastocyanin and stellacyanin. Dalton Transactions (25), 3067-3067

Antonyuk, S., Elam, JS., Hough, MA., Strange, RW., Doucette, PA., Rodriguez, JA., Hayward, LJ., Valentine, JS., Hart, PJ. and Hasnain, SS., (2005). Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg. Protein Science. 14 (5), 1201-1213

Hough, MA., Ellis, MJ., Antonyuk, S., Strange, RW., Sawers, G., Eady, RR. and Samar Hasnain, S., (2005). High Resolution Structural Studies of Mutants Provide Insights into Catalysis and Electron Transfer Processes in Copper Nitrite Reductase. Journal of Molecular Biology. 350 (2), 300-309

Hough, MA., Grossmann, JG., Antonyuk, SV., Strange, RW., Doucette, PA., Rodriguez, JA., Whitson, LJ., Hart, PJ., Hayward, LJ., Valentine, JS. and Hasnain, SS., (2004). Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants. Proceedings of the National Academy of Sciences. 101 (16), 5976-5981

Barrett, ML., Harris, RL., Antonyuk, S., Hough, MA., Ellis, MJ., Sawers, G., Eady, RR. and Hasnain, SS., (2004). Insights into Redox Partner Interactions and Substrate Binding in Nitrite Reductase fromAlcaligenes xylosoxidans: Crystal Structures of the Trp138His and His313Gln Mutants†,‡. Biochemistry. 43 (51), 16311-16319

Strange, RW., Antonyuk, S., Hough, MA., Doucette, PA., Rodriguez, JA., Hart, PJ., Hayward, LJ., Valentine, JS. and Hasnain, SS., (2003). The Structure of Holo and Metal-deficient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis. Journal of Molecular Biology. 328 (4), 877-891

Hough, MA. and Hasnain, SS., (2003). Structure of Fully Reduced Bovine Copper Zinc Superoxide Dismutase at 1.15 Å. Structure. 11 (8), 937-946

Kanbi, LD., Antonyuk, S., Hough, MA., Hall, JF., Dodd, FE. and Hasnain, SS., (2002). Crystal Structures of the Met148Leu and Ser86Asp Mutants of Rusticyanin from Thiobacillus ferrooxidans: Insights into the Structural Relationship with the Cupredoxins and the Multi Copper Proteins. Journal of Molecular Biology. 320 (2), 263-275

Hough, MA., Hall, JF., Kanbi, LD. and Hasnain, SS., (2001). Structure of the M148Q mutant of rusticyanin at 1.5 Å: a model for the copper site of stellacyanin. Acta Crystallographica Section D Biological Crystallography. 57 (3), 355-360

Hough, MA., Strange, RW. and Hasnain, SS., (2000). Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function. Journal of Molecular Biology. 304 (2), 231-241

Ockwell, DM., Hough, MA., Grossmann, JG., Hasnain, SS. and Hao, Q., (2000). Implementation of cluster analysis forab initiophasing using the molecular envelope from solution X-ray scattering. Acta Crystallographica Section D Biological Crystallography. 56 (8), 1002-1006

Hough, MA. and Hasnain, SS., (1999). Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal. Journal of Molecular Biology. 287 (3), 579-592

Conferences (2)

Sen, K., Hough, MA., Yong, CW., Keal, TW. and Strange, RW., (2017). Solvent accessibility and ligand binding in AcNiR, a two domain copper nitrite reductase

Horrell, S., Kekilli, D., Sen, K., Yong, CW., Keal, TW., Hough, MA. and Strange, RW., (2017). Multiple structures from one crystal serial crystallography (MSOX): variable temperature movies

Grants and funding

2018

High hit-rate, high-throughput serial protein crystallography at SACLA using fixed target silicon nitride chips

Biotechnology and Biological Sciences Research Council

2017

Bioimaging of dehydroascorbate and (phospho)lipid hydroperoxides: The development of fluorescent protein biosensors

Biotechnology & Biology Science Res.Council

2016

Development of methods and instrumentation for collection, analysis and validation of damage-free protein structures in defined redox states

Diamond Light Source Ltd

2015

Dynamics of Electron and Proton Transfer Chemistry in Copper and Hybrid Copper-Haem Enzymes

Biotechnology & Biology Science Res.Council

2014

Exploring the Role of a Dihydrolipoyl Dehydrogenase in the Breakdown of Naphthenic Acids

Biochemical Society

Biomedical Vacation Scholarships - 2014 (Miss R A Black)

Wellcome Trust

Enzyme Catalysis in Action: 3D Movies of X-ray Induced Chemical Reactions in Protein Crystals

Leverhulme Trust

2013

A novel monomeric cytochrome c' as a model for guanylate cyclase

Wellcome Trust

2012

A Cross-Species Approach to Understanding Ligrand Binding and Discrimination Nechanisms in Cytochromes c

The Royal Society

Contact

mahough@essex.ac.uk
+44 (0) 1206 873317

Location:

3SW.5.15B, Colchester Campus