Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp PCC 7120

被引:74
作者
Baniulis, Danas [1 ]
Yamashita, Eiki [2 ]
Whitelegge, Julian P. [4 ]
Zatsman, Anna I. [3 ]
Hendrich, Michael P. [3 ]
Hasan, S. Saif [1 ]
Ryan, Christopher M. [4 ]
Cramer, William A. [1 ]
机构
[1] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA
[2] Osaka Univ, Inst Prot Res, Osaka 5600043, Japan
[3] Carnegie Mellon Univ, Dept Chem, Pittsburgh, PA 15213 USA
[4] Univ Calif Los Angeles, NPI Semel Inst, Pasarow Mass Spectrometry Lab, Los Angeles, CA 90095 USA
基金
美国国家卫生研究院;
关键词
MEMBRANE-PROTEIN; OXIDOREDUCTASE ACTIVITY; SPINACH-CHLOROPLASTS; ANGSTROM RESOLUTION; ELECTRON-TRANSFER; PHOTOSYSTEM-II; ACETYLATION; ANABAENA; HEME; PHOTOSYNTHESIS;
D O I
10.1074/jbc.M809196200
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 crystal structure of the cyanobacterial cytochrome b(6)f complex has previously been solved to 3.0-angstrom resolution using the thermophilic Mastigocladus laminosus whose genome has not been sequenced. Several unicellular cyanobacteria, whose genomes have been sequenced and are tractable for mutagenesis, do not yield b(6)f complex in an intact dimeric state with significant electron transport activity. The genome of Nostoc sp. PCC 7120 has been sequenced and is closer phylogenetically to M. laminosus than are unicellular cyanobacteria. The amino acid sequences of the large core subunits and four small peripheral subunits of Nostoc are 88 and 80% identical to those in the M. laminosus b(6)f complex. Purified b6f complex from Nostoc has a stable dimeric structure, eight subunits with masses similar to those of M. laminosus, and comparable electron transport activity. The crystal structure of the native b6f complex, determined to a resolution of 3.0 angstrom (PDB id: 2ZT9), is almost identical to that of M. laminosus. Two unique aspects of the Nostoc complex are: (i) a dominant conformation of heme b(p) that is rotated 180 about the alpha- and gamma-meso carbon axis relative to the orientation in the M. laminosus complex and (ii) acetylation of the Rieske iron-sulfur protein (PetC) at the N terminus, a post-translational modification unprecedented in cyanobacterial membrane and electron transport proteins, and in polypeptides of cytochrome bc complexes from any source. The high spin electronic character of the unique heme c(n) is similar to that previously found in the b(6)f complex from other sources.
引用
收藏
页码:9861 / 9869
页数:9
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