Structure of a novel c7-type three-heme cytochrome domain from a multidomain cytochrome c polymer

被引:35
作者
Pokkuluri, PR
Londer, YY
Duke, NEC
Erickson, J
Pessanha, M
Salgueiro, CA
Schiffer, M
机构
[1] Argonne Natl Lab, Biosci Div, Argonne, IL 60439 USA
[2] Univ Nova Lisboa, Inst Tecnol Quim & Biol, P-2780156 Oeiras, Portugal
[3] Univ Nova Lisboa, Fac Ciencias & Tecnol, Dept Quim, P-2825114 Monte De Caparica, Portugal
关键词
multiheme cytochrome c; cytochrome c(7); Geobacter metallireducens; Geobacter sulfurreducens; heme coordination in c-type cytochromes; protein structure;
D O I
10.1110/ps.04626204
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The structure of a novel c(7)-type cytochrome domain that has two bis-histidine coordinated hemes and one heme with histidine, methionine coordination (where the sixth ligand is a methionine residue) was deter-mined at 1.7 Angstrom resolution. This domain is a representative of domains that form three polymers encoded by the Geobacter sulfurreducens genome. Two of these polymers consist of four and one protein of nine c(7)-type domains with a total of 12 and 27 hemes, respectively. Four individual domains (termed A, B C, and D) from one Such multiheme cytochrome c (ORF03300) were cloned and expressed in Escherichia coli. The domain C produced diffraction quality crystals from 2.4 M sodium malonate (pH 7). The Structure was solved by MAD method and refined to an R-factor of 19.5% and R-free of 21.8%. Unlike the two c(7) molecules with known structures, one from G. sulfurreducens (PpcA) and one from Desulfuromonas acetoxidans where all three hemes are bis-histidine coordinated, this domain contains a heme which is coordinated by a methionine and a histidine residue. As a result, the corresponding heme could have a higher potential than the other two hemes. The apparent midpoint reduction potential, E-app, of domain C is -105 mV, 50 mV higher than that of PpcA.
引用
收藏
页码:1684 / 1692
页数:9
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