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> ABRC Home > People List > John W. Peters
FACULTY > John W. Peters
John W. Peters, PI and Director of the ABRC
Research Interests
Research in the Peters’ group is focused at the biochemical level on understanding the structural and functional determinants of biological nitrogen fixation and hydrogen metabolism and at the genomic and environmental level on understanding the ecological occurrence and molecular evolution of these processes.
 Nitrogenases and hydrogenases catalyze exist as complex iron-sulfur enzymes with unique cofactors that have been proposed to be of the earliest cofactors. Our biochemical studies are aimed at providing insights into defining the structural determinants for catalysis (with Robert Szilagyi) and how these clusters are synthesized in biological systems (with Joan Broderick). The studies provide the basis for examining whether abiotic minerals can be tuned to have similar reactivity and catalytic properties in the hopes of getting a better handle on how modified iron-sulfur minerals functioned in the Hadean Earth to facilitate the origin of life. We use a variety of biochemical and spectroscopic approaches to examine these metal centers during catalysis and we examine specific poised states using structure determination by X-ray diffraction methods.
In other complementary work we are probing the limits of biological hydrogen metabolism and nitrogen fixation on Earth by using specific probes for hydrogenase and nitrogenase components in extreme environments. The ecolgoical studies involve the development of PCR gene amplification probes that are based on functionally important conserved regions of various hydrogenase and nitrogenase components. Amplification of hydrogenase and nitrogenase genes from environmental samples provides the basis to parameterize occurrence of these processes in nature and subsequent sequencing and phylogenic analysis reveals what environments favor deeply rooted lineages. The evolution of hydrogenases and nitrogenases appear to be very interesting and represent classic cases of convergent (hydrogenases) and divergent (nitrogenases) evolution. A variety of different approaches are being used to study evolutionary relationships keying on specific evolutionary events such as gene duplication and gene fusion events.
Selected Publications
R. Sarma, B.M. Barney, T.L. Hamilton, A. Jones, L.C. Seefeldt, and J.W. Peters “Crystal Structure of the L Protein of Rhodobacter sphaeroides Light-Independent Protochlorophyllide Reductase with MgADP Bound: A Homologue of the Nitrogenase Fe Protein” Biochemistry – Epub (2008)
S.E. McGlynn, E.M. Shepard, M.A. Winslow, AV. Naumov, K.S. Duschene, M.C. Posewitz, W.E. Broderick, J.B. Broderick, and J.W. Peters “HydF as a Scaffold in [FeFe] Hydrogenase H-Cluster Biosynthesis” FEBS Letters 582, 2183-2187. (2008)
A.-S. Steunou, S.I. Jensen, E. Brecht, M.M. Bateson, O. Killian, D. Bhaya, D.M. Ward, J.W.Peters, A.R. Grossman, and M. Kühl “Regulation of nif Gene Expression and the Energetics of Cyanobacterial N2 Fixation Over the Diel Cycle in a Hot Spring Microbial Mat” ISME J. 2:364-378 (2008)
A.S. Pandey, T. Harris, L. Giles, J.W. Peters, and R.K. Szilagyi. Dithiomethylether as a Ligand in the Hydrogen H-Cluster. JACS 130:4533-4540 (2008)
R. Sarma, D.M. Mulder, E. Brecht, L.C. Seefeldt, R.K. Szilagyi, H. Tsuruta, and J.W. Peters. Mapping Nitrogenase Fe Protein Conformational Change in Solution Using Small Angle X-Ray Scattering. Biochemistry 46, 14058-14066 (2007)
S. McGlynn, S.S. Ruebush, A.V. Naumov, L.E. Nagy, A. Dubini, P.W. King, J.B. Broderick, M.C. Posewitz, and J.W. Peters. In vitro activation fo [FeFe] hydrogenase: New insights into hydrogenase maturation. JBIC 12(4) 443-447 (2007)
J.W. Peters, R.K. Szilagyi, A.V. Naumov, and T. Douglas “A Radical Solution for the Biosynthesis of the H cluster of Hydrogenase” FEBS Letters 580, 363-367 (2006)
D.E. Schwab, C. Tard, E. Brecht, J.W. Peters, C.J. Pickett, and R.K. Szilagyi. Delocalized Electronic Structure of Hydrogenase H-cluster Probed by X-ray Absorption Spectroscopy and Density Functional Theory. 3696-3698 Chem. Comm. (2006)
S. Sen, A.M. Krishnakumar J. McClead, L.C. Seefeldt and J.W. Peters. Insights Into the Role of Nucleotide Dependent Conformational Change in Nitrogenase Catalysis: Structural Characterization of the Nitrogenase Fe protein Leu127 Deletion Variant with Bound MgATP. J. Inorg. Biochem. 100, 1041-1052 (2006)
S. Sen, and J.W. Peters. The Thermal Adaptation of the Nitrogenase Fe protein from Thermophilic Methanobacter thermoautotrophicus. Proteins 62, 450-460 (2006)
Lab Personnel
Eric Boyd
Post-doctoral Associate
eboyd@montana.edu
Shawn McGlynn*
Graduate Student
simplyshawn@gmail.com
David Mulder
Graduate Student
dmulder@gmail.com
Trinity Hamilton
Graduate Student
tri_lynn@msn.com
Ranjana Sarma
Graduate Student
rsarma@chemistry.montana.edu
Jesse Therien
Graduate Student
jesse_therien@hotmail.com
Collaborators
Lance Seefelt (Nitrogenase Biochemistry)
Department of Chemistry and Biochemistry
Utah State University
Mark Skidmore (Subglacial geology and ecology)
Department of Earth Sciences
Montana State University
Stephen Cramer (X-ray spectroscopy)
Department of Applied Science
University of California at Davis
John Leigh (Nif Regulation in Methanogens)
Department of Microbiology
University of Washington
John Spear (Microbial Ecology)
Department of Environmental Science and Engineering
Colorado School of Mines
Donald Bryant (Photosynthesis)
Department of Biochemistry and Molecular Biology
Pennsylvania State University
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