Abstract

We propose to carry out detailed physical-chemical studies of cytochrome c1aa3 and the Rieske iron-sulfur protein isolated from the extremely thermophilic, aerobic bacterium, Thermus thermophilus. Preliminary studies have shown that the functional components of these proteins are identical to analogous proteins obtained from mitochondria. Our studies take advantage of bacterial metabolism to specifically introduce probe atoms into the molecules of interest, and our experiments will lead to new knowledge of the active-site structures of these proteins and how they function. The work proposed for this grant period is planned to supply information and materials from which to construct a """"""""minimum component"""""""" respiratory system. It is suggested that proteins obtained from extreme thermophiles, because of their resistance to denaturation, are ideal subjects for detailed examination of mechanisms in respiration.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM035342-03
Application #
3287933
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1984-12-01
Project End
1988-02-29
Budget Start
1986-12-01
Budget End
1988-02-29
Support Year
3
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

McDonald, William; Funatogawa, Chie; Li, Yang et al. (2014) Conserved glycine 232 in the ligand channel of ba3 cytochrome oxidase from Thermus thermophilus. Biochemistry 53:4467-75
McDonald, William; Funatogawa, Chie; Li, Yang et al. (2013) Ligand access to the active site in Thermus thermophilus ba(3) and bovine heart aa(3) cytochrome oxidases. Biochemistry 52:640-52
Luna, V Mitch; Fee, James A; Deniz, Ashok A et al. (2012) Mobility of Xe atoms within the oxygen diffusion channel of cytochrome ba(3) oxidase. Biochemistry 51:4669-76
Neehaul, Yashvin; Chen, Ying; Werner, Carolin et al. (2012) Electrochemical and infrared spectroscopic analysis of the interaction of the Cu(A) domain and cytochrome c(552) from Thermus thermophilus. Biochim Biophys Acta 1817:1950-4
Chang, Hsin-Yang; Choi, Sylvia K; Vakkasoglu, Ahmet Selim et al. (2012) Exploring the proton pump and exit pathway for pumped protons in cytochrome ba3 from Thermus thermophilus. Proc Natl Acad Sci U S A 109:5259-64
Egawa, Tsuyoshi; Chen, Ying; Fee, James A et al. (2012) The rate-limiting step in O(2) reduction by cytochrome ba(3) from Thermus thermophilus. Biochim Biophys Acta 1817:666-71
Liu, Bin; Zhang, Yang; Sage, J Timothy et al. (2012) Structural changes that occur upon photolysis of the Fe(II)(a3)-CO complex in the cytochrome ba(3)-oxidase of Thermus thermophilus: a combined X-ray crystallographic and infrared spectral study demonstrates CO binding to Cu(B). Biochim Biophys Acta 1817:658-65
Tiefenbrunn, Theresa; Liu, Wei; Chen, Ying et al. (2011) High resolution structure of the ba3 cytochrome c oxidase from Thermus thermophilus in a lipidic environment. PLoS One 6:e22348
Smirnova, Irina; Reimann, Joachim; von Ballmoos, Christoph et al. (2010) Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus. Biochemistry 49:7033-9
Moënne-Loccoz, Pierre; Fee, James A (2010) Biochemistry. Catalyzing NO to N2O in the nitrogen cycle. Science 330:1632-3

Showing the most recent 10 out of 41 publications