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> Home > Faculty
& Staff > Dr. John W. Peters
Hydrogen Metabolism and Nitrogen Fixation in Thermal Environments
Our primary interests are structure/function relationships in metal-containing
proteins. A variety of approaches including x-ray diffraction techniques
are used to probe aspects of the mechanism of a number of interesting bioconversions. In
these studies three-dimensional structures serve as a basis for understanding
the molecular mechanisms of enzyme-catalyzed reactions. Our current areas
of active research are hydrogen metabolism, nitrogen metabolism, carbon dioxide
fixation, metal reduction, and biodegradation of aliphatic ketones and epoxides.
Our Thermal Biology related research is focused on the isolation and characterization
of complex metal-containing enzymes from microorganisms existing in the thermal
environments in Yellowstone National Park. The current thrust of this
research is the identification and characterization of enzymes involved nitrogen
metabolism, hydrogen metabolism, and metal reduction. In addition to
this research we are initiating work to develop model systems for the study
of aspects of enzyme thermal adaptation with a particular emphasis on adaptation
occurring at the level of protein structure.
Topology
of the overall fold CpI, divided into four structural domains on the basis
of the location of protein-associated [Fe-S] clusters and sequence similarity
of the individual domains to individual domain or free proteins. The active-site
domain is shown in cyan; a second domain with two [4Fe-4S] clusters is shown
in rust, a third domain with a single [4Fe-4S] cluster is shown is green and
a fourth domain with a single [2Fe-4S] cluster is shown in blue. The [Fe-S]
clusters are represented as space-filling models (Fe, rust; S, yellow). (Peters
Research Group, image)
CpI
active site H cluster and coordinating Cys ligands located at the boundary
of the two lobes of the active-site domain. The active-site cluster is covalently
bound to the proteins through four cysteine S atoms (yellow) that are bound
to five Fe atoms (rust). The CO/CN molecules, which serve as ligands to the
[2Fe] subcluster of the active-site cluster, are all represented as carbonyls
(C, black; O, red). The two Fe atoms are labeled 1 and 2 and are located at
a refined distance of 2.62 ? with respect to one another. Additional ligands
to the Fe atoms of this subcluster include two bridging S atoms (yellow) and
a terminally bound water molecule (red). A covalent linkage of unknown light
atoms as a component of a biologically unique dithiolate ligand is shown in
magenta. (Peters Research Group, image)
Current Laboratory Personnel
Dr. Anatoli Naumov, Postdoctoral Associate
Dr. Shane Ruebush, Postdoctoral Associate
Dr. Oleg Zadvorney, Postdoctoral Associate
Arathi Krishnakumar, Ph.D. Student
Shawn McGlynn, Ph.D. Student
David Mulder, Ph.D. Student
Arti Pandey, Ph.D. Student
Ranjana Sarma, Ph.D. Student
Jesse Therien, Ph.D. Student
Christian Coe, Undergraduate Student
Kevin Swanson, Undergraduate Student
Eric Brecht, Laboratory Manager
The Peters lab group
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