Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Michelle A. Pressler"'
Autor:
David L. DeWitt, Joseph F. Leykam, Michelle A. Pressler, Gerald T. Babcock, Catherine DeMaso, Denis A. Proshlyakov
Publikováno v:
Science. 290:1588-1591
Cytochrome oxidase activates and reduces O 2 to water to sustain respiration and uses the energy released to drive proton translocation and adenosine 5′-triphosphate synthesis. A key intermediate in this process, P , lies at the junction of the O 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2819ad676bf5aba92f792af5f7af57bf
https://doi.org/10.1126/science.290.5496.1588
https://doi.org/10.1126/science.290.5496.1588
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365(1-2):170-174
We propose that the interconversions of water and oxygen are catalyzed by the transition metal ions of Photosystem II and cytochrome c oxidase in remarkably similar ways. Oxygen-oxygen bond formation and cleavage occurs between two oxygen atoms that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa401a32a049d875dc7318a1b5e3f921
Autor:
Christopher M. Colangelo, Gerard J. Colpas, Michelle A. Pressler, Robert P. Hausinger, Timothy G. Brayman, Gerald T. Babcock, John McCracken, Li June Ming, Robert A. Scott
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 3:150-160
The urease accessory protein encoded by ureE from Klebsiella aerogenes is proposed to function in Ni(II) delivery to the urease apoprotein. Wild-type UreE contains a histidine-rich region at its carboxyl terminus and binds 5–6 Ni per dimer, whereas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::53a82bd3743fff97ff43bcaba25f19d0
https://doi.org/10.1007/s007750050216
https://doi.org/10.1007/s007750050216
Autor:
Shelagh Ferguson-Miller, Curt Hoganson, Jie Qian, Gerald T. Babcock, Denise A. Mills, Wenjun Shi, Michelle A. Pressler
Publikováno v:
Biochemistry. 36:2539-2543
Several pathways for proton transport in cytochrome c oxidase have been proposed on the basis of mutational analysis and X-ray structure: at least one for moving "pumped" protons from the interior to exterior of the membrane and a separate route for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::acfa8c469e433c0f17e01942ec1d7024
https://doi.org/10.1021/bi962721+
https://doi.org/10.1021/bi962721+
Autor:
John Fetter, Bo G. Malmström, Shelagh Ferguson-Miller, Jonathan P. Hosler, David M. Mitchell, James O. Alben, Gerald T. Babcock, Roland Aasa, Peter Brzezinski, Robert B. Gennis, Michelle A. Pressler, Pia Ädelroth
Publikováno v:
Biochemistry. 35:824-828
The molecular mechanism by which proton pumping is coupled to electron transfer in cytochrome c oxidase has not yet been determined. However, several models of this process have been proposed which are based on changes occurring in the vicinity of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1fc22327f4cdbfc3022da1f165374a9
https://doi.org/10.1021/bi951897t
https://doi.org/10.1021/bi951897t
Autor:
Shelagh Ferguson-Miller, Peter Brzezinski, James O. Alben, Denise A. Mills, Bo G. Malmström, David M. Mitchell, Youngkyou Kim, John Fetter, Pia Ädelroth, Roland Aasa, Michelle A. Pressler, Gerald T. Babcock, Robert B. Gennis
Publikováno v:
Biochemistry. 35:13089-13093
Several putative proton transfer pathways have been identified in the recent crystal structures of the cytochrome oxidases from Paracoccus denitrificans [Iwata et al. (1995) Nature 376, 660-669] and bovine [Tsukihara (1996) Science 272, 1138-1144]. A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::082031dab38814109889a5570f630760
https://doi.org/10.1021/bi961416l
https://doi.org/10.1021/bi961416l
Autor:
Suranjan Bhanja Choudhury, Michelle A. Pressler, Michael J. Maroney, Shaukat A. Mirza, Roberta O. Day
Publikováno v:
Inorganic Chemistry. 33:4831-4839
The syntheses, structures, and redox properties of isomorphous Ni(I1) thiolato and selenolato complexes of the tridentate ligands bis(2-(hydrochalcogeno)ethyl)methylamines are reported. Reaction of Ni(0Ac)z with bis(2mercaptoethy1)methylamine leads t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::30415a8552b1c88ce99527de8e208165
https://doi.org/10.1021/ic00100a005
https://doi.org/10.1021/ic00100a005
Publikováno v:
Inorganic Chemistry. 32:977-987
The reactions of Ni complexes of the tridentate dithiolate ligands RN(CH 2 CH 2 S - ) 2 and S(CH 2 CH 2 S - ) 2 with O 2 leading to the formation of complexes containing one S-hound sulfinate ligand are described. Reaction of the ligands with Ni(OAc)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e922a6de9e8c0f84a5caef12610688b2
https://doi.org/10.1021/ic00058a038
https://doi.org/10.1021/ic00058a038
Publikováno v:
Biochemistry. 38(49)
The catalytic core of cytochrome c oxidase is composed of three subunits: I, II, and III. Subunit III is a highly hydrophobic membrane protein that contains no redox centers; its role in cytochrome oxidase function is not obvious. Here, subunit III h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6890e3df334a6b490007fe811789a3f4
https://pubmed.ncbi.nlm.nih.gov/10587446
https://pubmed.ncbi.nlm.nih.gov/10587446
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 95(14)
Elucidating the structures of intermediates in the reduction of O 2 to water by cytochrome c oxidase is crucial to understanding both oxygen activation and proton pumping by the enzyme. In the work here, the reaction of O 2 with the mixed-valence enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5a060713c541e50f3cb4c58ea175140
https://pubmed.ncbi.nlm.nih.gov/9653133
https://pubmed.ncbi.nlm.nih.gov/9653133