Abstract

This renewal proposal will provide information on the factors which control reaction rates and reaction specificity in protein-protein electron transfer reactions. Such reactions are centrally important in controlling biological energy flow in the electron transport/oxidative phosphorylation system, and also play an important role in many metabolic reactions. We will monitor the kinetics of reactions in the cytc/cyt c peroxidase complex, the cyt b5: hemoglobin (myoglobin) complexes, and the cytc:cyt c1 complex, using a variety of methods developed in our lab with a particular focus on photochemical electron transfer. Concomittantly, structural studies will be pursued to learn about the nature of binding and recognition in these electron transfer protein complexes, and to probe the dynamic behavior of the structure of such protein complexes. Two novel methods have been developed for such studies, focusing on NMR and energy transfer techniques, respectively.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM033881-06
Application #
3284023
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1985-09-05
Project End
1994-11-30
Budget Start
1991-12-01
Budget End
1992-11-30
Support Year
6
Fiscal Year
1992
Total Cost
Indirect Cost

  Institution

Name
University of Rochester
Department
Type
Schools of Arts and Sciences
DUNS #
208469486
City
Rochester
State
NY
Country
United States
Zip Code
14627

  Publications

Drel, Viktor R; Pacher, Pal; Vareniuk, Igor et al. (2007) A peroxynitrite decomposition catalyst counteracts sensory neuropathy in streptozotocin-diabetic mice. Eur J Pharmacol 569:48-58
Wheeler, Daniel S; Miller, Ralph R (2005) Recovery from blocking between outcomes. J Exp Psychol Anim Behav Process 31:467-76
Doerr, Allison J; McLendon, George L (2004) Design, folding, and activities of metal-assembled coiled coil proteins. Inorg Chem 43:7916-25
Springs, Stacy L; Bass, Susanna E; Bowman, Greg et al. (2002) A multigeneration analysis of cytochrome b(562) redox variants: evolutionary strategies for modulating redox potential revealed using a library approach. Biochemistry 41:4321-8
Springs, S L; Bass, S E; McLendon, G L (2000) Cytochrome b562 variants: a library for examining redox potential evolution. Biochemistry 39:6075-82
McLendon, G; Feitelson, J (1994) Electron-transfer reactions of hemoglobin with small molecules: a potential probe of conformational dynamics. Methods Enzymol 232:86-94
Corin, A F; Hake, R A; McLendon, G et al. (1993) Effects of surface amino acid replacements in cytochrome c peroxidase on intracomplex electron transfer from cytochrome c. Biochemistry 32:2756-62
McLendon, G L; Bagby, S; Charman, J A et al. (1991) Subunit interactions change the heme active-site geometry in p-cresol methylhydroxylase. Proc Natl Acad Sci U S A 88:9463-7
Corin, A F; McLendon, G; Zhang, Q et al. (1991) Effects of surface amino acid replacements in cytochrome c peroxidase on complex formation with cytochrome c. Biochemistry 30:11585-95
Feitelson, J; McLendon, G (1991) Migration of small molecules through the structure of hemoglobin: evidence for gating in a protein electron-transfer reaction. Biochemistry 30:5051-5

Showing the most recent 10 out of 14 publications