Abstract

The long-term goal of this proposal is the characterization of the structural dynamics that accompany electron transfer at the active sites of heme proteins and protein complexes. This will allow us to determine the molecular mechanisms by which this important physiological process is regulated during respiration in living cells. We will employ time-resolved optical spectroscopies to follow electron transfer dynamics on appropriate timescales. Components of the mitochrondrial electron transport chain, specifically cytochrome c oxidase and bc1 complexes, will be investigated using time-resolved resonance Raman techniques already available in our laboratory. Several new classes of photoactive molecules will be used to initiate electron flow with protein systems that have been poised in specific redox or reactive states. This technique will permit us to isolate and characterize the extent to which protein conformational dynamics control the rate and specificity of electron flow in multi-component complexes.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM033330-09
Application #
3282912
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1984-07-01
Project End
1996-06-30
Budget Start
1992-07-01
Budget End
1993-06-30
Support Year
9
Fiscal Year
1992
Total Cost
Indirect Cost

  Institution

Name
University of New Mexico
Department
Type
Schools of Arts and Sciences
DUNS #
829868723
City
Albuquerque
State
NM
Country
United States
Zip Code
87131

  Publications

Gao, F; Qin, H; Knaff, D B et al. (1999) Q-Band resonance Raman investigation of turnip cytochrome f and Rhodobacter capsulatus cytochrome c1. Biochim Biophys Acta 1430:203-13
Gao, F; Qin, H; Knaff, D B et al. (1998) Q-band resonance Raman spectra of oxidized and reduced mitochondrial bc1 complexes. Biochemistry 37:9751-8
Simpson, M C; Millett, F; Pan, L P et al. (1996) Transient and time-resolved resonance Raman investigation of photoinitiated electron transfer in ruthenated cytochromes c. Biochemistry 35:10019-30
Wang, J; Larsen, R W; Moench, S J et al. (1996) Cytochrome c peroxidase complexed with cytochrome c has an unperturbed heme moiety. Biochemistry 35:453-63
Gao, F; Qin, H; Simpson, M C et al. (1996) Isolation and characterization of vibrational spectra of individual heme active sites in cytochrome bc1 complexes from Rhodobacter capsulatus. Biochemistry 35:12812-9
Garcia Castillo, M C; Lou, B S; Ondrias, M R et al. (1994) Characterization of flavocytochrome C552 from the thermophilic photosynthetic bacterium Chromatium tepidum. Arch Biochem Biophys 315:262-6
Schneebeck, M C; Vigil, L E; Friedman, J M et al. (1993) Heme-CO religation in photolyzed hemoglobin: a time-resolved Raman study of the Fe-CO stretching mode. Biochemistry 32:1318-23
Lou, B S; Hobbs, J D; Chen, Y R et al. (1993) Structural characterization of isolated mitochondrial cytochrome c1. Biochim Biophys Acta 1144:403-10
Hirasawa, M; Chang, K T; Dose, M M et al. (1993) Characterization of two low-potential cytochromes from bean sprouts. Biochim Biophys Acta 1141:253-61
Wang, J; Zhu, H; Ondrias, M R (1992) Protein conformational perturbations affect the photoreduction of native cytochrome c peroxidase (III) at alkaline pH. Biochemistry 31:12847-54

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