Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Lois Geren"'
Autor:
Sue Ellen Brand, Martha Scharlau, Lois Geren, Marissa Hendrix, Clayre Parson, Tyler Elmendorf, Earl Neel, Kaila Pianalto, Jennifer Silva-Nash, Bill Durham, Francis Millett
Publikováno v:
Cells, Vol 11, Iss 24, p 4014 (2022)
Cytochrome c (Cc) underwent accelerated evolution from the stem of the anthropoid primates to humans. Of the 11 amino acid changes that occurred from horse Cc to human Cc, five were at Cc residues near the binding site of the Cc:CcO complex. Single-p
Externí odkaz:
https://doaj.org/article/60c0654cabbb4f038c731df6eb77afda
Autor:
Eugene Y. Zhen, Ray Rajagukguk, Martha Scharlau, Bill Durham, Lois Geren, Ling Ma, Shelagh Ferguson-Miller, Francis Millett
Publikováno v:
Biochemistry. 58(40)
The reaction between cytochrome c (Cc) and cytochrome c oxidase (CcO) was studied using horse cytochrome c derivatives labeled with ruthenium trisbipyridine at Cys 39 (Ru-39-Cc). Flash photolysis of a 1:1 complex between Ru-39-Cc and bovine CcO at a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2f7f353954e2872a568371b9d25db5a
https://pubmed.ncbi.nlm.nih.gov/31532642
https://pubmed.ncbi.nlm.nih.gov/31532642
Autor:
Eugene Y. Zhen, Martha Scharlau, Lois Geren, Francis Millett, Ling Ma, Shelagh Ferguson-Miller, Bill Durham, Ray Rajagukguk
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859:e71
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::020caec53b7c25d4b9771ed7ae7b9e4d
https://doi.org/10.1016/j.bbabio.2018.09.213
https://doi.org/10.1016/j.bbabio.2018.09.213
Autor:
Shelagh Ferguson-Miller, Carrie Hiser, Bill Durham, John McCracken, Shujuan Xu, Lois Geren, Martyn A. Sharpe, Francis Millett, Denise A. Mills, Ling Qin
Publikováno v:
Biochemistry. 47:11499-11509
Eukaryotic cytochrome c oxidase (CcO) and homologous prokaryotic forms of Rhodobacter and Paraccocus differ in the EPR spectrum of heme a. It was noted that a histidine ligand of heme a (H102) is hydrogen bonded to serine in Rhodobacter (S44) and Par
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc1d291485e7215b6790b2e7b2d55ca4
https://doi.org/10.1021/bi801156s
https://doi.org/10.1021/bi801156s
Autor:
Lois Geren, Bryan Schmidt, Shelagh Ferguson-Miller, Bill Durham, Carrie Hiser, Francis Millett, Denise A. Mills
Publikováno v:
Biochemistry. 44:10457-10465
Cytochrome c oxidase pumps protons across a membrane using energy from electron transfer and reduction of oxygen to water. It is postulated that an element of the energy transduction mechanism is the movement of protons to the vicinity of the hemes u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa086284dcc393c210895e18236033de
https://doi.org/10.1021/bi050283d
https://doi.org/10.1021/bi050283d
Autor:
Robert C. Sadoski, Francis Millett, Dmitry Zaslavsky, Lois Geren, Bill Durham, Sany Rajagukguk, Robert B. Gennis
Publikováno v:
Proceedings of the National Academy of Sciences. 101:10544-10547
The mechanism by which electron transfer is coupled to proton pumping in cytochrome c oxidase is a major unsolved problem in molecular bioenergetics. In this work it is shown that, at least under some conditions, proton release from the enzyme occurs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4f8823a3d92c63aa467b4e728926dad
https://doi.org/10.1073/pnas.0401521101
https://doi.org/10.1073/pnas.0401521101
Autor:
Kefei Wang, Ling Ma, Yuejun Zhen, Shelagh Ferguson-Miller, Lois Geren, Bill Durham, Francis Millett
Publikováno v:
Biochemistry. 41:2298-2304
The function of the binuclear Cu(A) center in cytochrome c oxidase (CcO) was studied using two Rhodobacter sphaeroides CcO mutants involving direct ligands of the Cu(A) center, H260N and M263L. The rapid electron-transfer kinetics of the mutants were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::381c65e73a16f60053270147487a0a69
https://doi.org/10.1021/bi0114630
https://doi.org/10.1021/bi0114630
Autor:
Lois Geren, Susan Grinnell, Kefei Wang, Robert C. Sadoski, Shelagh Ferguson-Miller, Bill Durham, Yuejun Zhen, Francis Millett
Publikováno v:
Journal of Biological Chemistry. 274:38042-38050
The reaction between cytochrome c(Cc) and Rhodobacter sphaeroides cytochrome coxidase (CcO) was studied using a cytochrome c derivative labeled with ruthenium trisbipyridine at lysine 55 (Ru-55-Cc). Flash photolysis of a 1:1 complex between Ru-55-Cc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::984cf77b355f57a108c760484460b29a
https://doi.org/10.1074/jbc.274.53.38042
https://doi.org/10.1074/jbc.274.53.38042
Design of ruthenium-cytochrome c derivatives to measure electron transfer to cytochrome c peroxidase
Autor:
Jill L. Fairris, Rui-Qin Liu, A. McKee, N. Peffer, Lois Geren, P. Anderson, Bill Durham, F.S. Millett
Publikováno v:
Biochimie. 77:549-561
A new technique has been introduced to measure interprotein electron transfer which involves photoexcitation of a tris(bipyridine)ruthenium (Ru) complex covalently attached to one of the proteins. Four different strategies have been developed to spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e000acec9e68b875db0a8e1732a7c76
https://doi.org/10.1016/0300-9084(96)88171-5
https://doi.org/10.1016/0300-9084(96)88171-5
Publikováno v:
Biochemistry. 33:1473-1480
The reactions of recombinant cytochrome c peroxidase [CcP(MI)] and a number of CcP(MI) mutants with native and ruthenium-labeled horse ferrocytochrome c have been studied by stopped-flow spectroscopy and laser flash photolysis. At 100 mM ionic streng
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ffd5305574f48518352876748e3fe7d
https://doi.org/10.1021/bi00172a025
https://doi.org/10.1021/bi00172a025