Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.
Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.
复制标题
细胞色素c氧化酶催化位点的定义:血红素a和血红素a3-CuB中心的特异性配体。
DOI:
10.1073/pnas.89.11.4786
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发表时间:
1992
影响因子:
11.1
通讯作者:
Ferguson-Miller,S
中科院分区:
文献类型:
--
作者:
Shapleigh,JP;Hosler,JP;Tecklenburg,MM;Kim,Y;Babcock,GT;Gennis,RB;Ferguson-Miller,S
The three-subunit aa3-type cytochrome c oxidase (EC 1.9.3.1) of Rhodobacter sphaeroides is structurally and functionally homologous to the more complex mitochondrial oxidase. The largest subunit, subunit I, is highly conserved and predicted to contain 12 transmembrane segments that provide all the ligands for three of the four metal centers: heme a, heme a3, and CuB. A variety of spectroscopic techniques identify these ligands as histidines. We have used site-directed mutagenesis to change all the conserved histidines within subunit I of cytochrome c oxidase from Rb. sphaeroides. Analysis of the membrane-bound and purified mutant proteins by optical absorption and resonance Raman spectroscopy indicates that His-102 and His-421 are the ligands of heme a, while His-284, His-333, His-334, and His-419 ligate the heme a3-CuB center. To satisfy this ligation assignment, helices II, VI, VII, and X, which contain these histidine residues, must be in close proximity. These data provide empirical evidence regarding the three-dimensional protein structure at the catalytic core of cytochrome c oxidase.