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首页> 外文期刊>Biochemistry >Redox Interaction of Cytochrome c_3 with [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F
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Redox Interaction of Cytochrome c_3 with [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F

机译：细胞色素c_3与寻常型脱硫弧菌宫崎骏F的[NiFe]氢化酶的氧化还原相互作用

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摘要

Cytochrome c_3 isolated from a sulfate-reducing bacterium,Desulfovibrio vulgaris Miyazaki F,is a tetraheme protein.Its physiological partner,[NiFe] hydrogenase,catalyzes the reversible oxidoreduction of molecular hydrogen.To elucidate the mechanism of electron transfer between cytochrome c_3 and [NiFe] hydrogenase,the transient complex formation by these proteins was investigated by means of NMR.All NH signals of uniformly ~(15)N-labeled ferric cytochrome c_3 except N-terminus,Pro,and Gly73 were assigned.~1H-~(15)N HSQC spectra were recorded for ~(l5)N-labeled ferric and ferrous cytochrome c_3,in the absence and presence of hydrogenase.Chemical shift perturbations were observed in the region around heme 4 in both oxidation states.Additionally,the region between hemes 1 and 3 in ferrous cytochrome c_3 was affected in the presence of hydrogenase,suggesting that the mode of interaction is different in each redox state.Heme 3 is probably the electron gate for ferrous cytochrome c_3.To investigate the transient complex of cytochrome c_3 and hydrogenase in detail,modeling of the complex was performed for the oxidized proteins using a docking program,ZDOCK 2.3,and NMR data.Furthermore,the roles of lysine residues of cytochrome c_3 in the interaction with hydrogenase were investigated by site-directed mutagenesis.When the lysine residues around heme 4 were replaced by an uncharged residue,methionine,one by one,the K_m of the electron-transfer kinetics increased.The results showed that the positive charges of Lys60,Lys72,Lys95,and Lysl0l around heme 4 are important for formation of the transient complex with [NiFe] hydrogenase in the initial stage of the cytochrome c_3 reduction.This finding is consistent with the most possible structure of the transient complex obtained by modeling.
机译：从硫酸盐还原菌宫崎骏F分离的细胞色素c_3是一种四血红素蛋白。其生理伴侣[NiFe]氢化酶催化分子氢的可逆氧化还原。 ]氢化酶，通过NMR研究了这些蛋白质形成的瞬时复合物。分配了〜（15）N标记的三价铁细胞色素c_3的所有NH信号，除了N-末端，Pro和Gly73。〜1H-〜（15在不存在和存在氢化酶的情况下，记录了〜（l5）N标记的三价铁和亚铁细胞色素c_3的N HSQC光谱。在两种氧化态下血红素4周围的区域均观察到化学位移扰动。此外，血红素之间的区域在存在氢化酶的情况下，亚铁细胞色素c_3中的1和3受到影响，这表明相互作用模式在每种氧化还原状态下都不同。血红素3可能是亚铁细胞色素c_3的电子门。详细地刺激细胞色素c_3和氢化酶的瞬时复合物，使用对接程序，ZDOCK 2.3和NMR数据对氧化的蛋白质进行了复合物的建模。此外，细胞色素c_3的赖氨酸残基在与氢化酶相互作用中的作用是通过定点诱变研究。当血红素4周围的赖氨酸残基被不带电荷的残基蛋氨酸一一取代时，电子转移动力学的K_m增大。结果表明，Lys60，Lys72，Lys95的正电荷，和血红素4周围的Lys101对在细胞色素c_3还原的初始阶段与[NiFe]氢化酶形成瞬态复合物很重要。这一发现与通过建模获得的最可能的瞬态复合物结构一致。

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