An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase.
about
Energy transduction: proton transfer through the respiratory complexesFast-forward genetics by radiation hybrids to saturate the locus regulating nuclear-cytoplasmic compatibility in TriticumCharacterizing the proton loading site in cytochrome c oxidase.Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidaseCommunication between R481 and Cu(B) in cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Functional importance of a pair of conserved glutamic acid residues and of Ca(2+) binding in the cbb(3)-type oxygen reductases from Rhodobacter sphaeroides and Vibrio cholerae.Redox-coupled proton pumping in cytochrome c oxidase: further insights from computer simulation.Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase.Proton-dependent electron transfer from CuA to heme a and altered EPR spectra in mutants close to heme a of cytochrome oxidase.Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump.Computational prediction and in vitro analysis of potential physiological ligands of the bile acid binding site in cytochrome c oxidaseThe rapid evolution of an ohnolog contributes to the ecological specialization of incipient yeast species.
P2860
Q22255654-55EF4B55-140F-4F9D-8943-69507AFD5E8BQ28821864-02F2433C-7FE3-4304-8604-0B74B16EF946Q34119860-75D77DBB-182A-437D-ADC0-3ACD91480CC5Q35633908-B1FEA4C6-8378-4E6D-916B-D96B58414C1EQ36163371-07EC8A91-9034-4DA0-BE13-E8D90A099105Q36336868-A5B39F9C-0E93-4F7B-8ED4-75DFF42C39C0Q36477773-FB85C519-29D9-4CFC-9842-D97A60BD1588Q36663543-A68BD3A7-F48B-4C3F-8A99-0BB7A3961992Q37137110-3696B476-5FCC-4F40-81B8-7C03555A7F6BQ37327646-5ADB17C2-462C-4417-B49A-1C5C0B2767DEQ37384663-D6CE78F8-7695-48BD-B441-669875852E7CQ38798074-F8242DCB-1F25-4CDD-B3B6-AF243F99AE85
P2860
An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@en
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@nl
type
label
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@en
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@nl
prefLabel
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@en
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@nl
P2093
P2860
P356
P1433
P1476
An arginine to lysine mutation ...... nsfer in cytochrome c oxidase.
@en
P2093
Bill Durham
Bryan Schmidt
Carrie Hiser
Denise A Mills
Francis Millett
Lois Geren
Shelagh Ferguson-Miller
P2860
P304
10457-10465
P356
10.1021/BI050283D
P407
P577
2005-08-01T00:00:00Z