Photosensitivity of the Ni-A state of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F with visible light.

Photosensitivity of the Ni-A state of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F with visible light.
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来自普通脱硫弧菌 Miyazaki F 的 [NiFe] 氢化酶的 Ni-A 态对可见光的光敏性。

DOI:
10.1016/j.bbrc.2012.10.136
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发表时间:
2013
影响因子:
3.1
通讯作者:
S. Hirota
S. Hirota
中科院分区:
生物学4区
文献类型:
--
作者:
H. Osuka;Y. Shomura;H. Komori;N. Shibata;S. Nagao;Y. Higuchi;S. Hirota

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氢化酶催化分子氢的可逆氧化。其活性位点由异核Ni - fe配合物构成,并且Ni离子的氧化态根据酶的氧化还原状态而变化。我们发现,来自于Desulfovibrio vulgaris Miyazaki F (DvMF)的[NiFe]氢化酶的Ni-A态(一种失活的未氧化态)是光敏的,在可见光照射下形成一个新的态(Ni-AL)。Ni-A态1956、2084和2094cm−1处的傅里叶变换红外(FT-IR)波段向Ni-AL态1971、2086和2098cm−1处偏移。室温下Ni-A态电子顺磁共振(EPR)谱信号的g值gx=2.30, gy=2.23, gz=2.01分别为- 0.009,+0.012和+0.010。在室温下,光诱导的Ni-AL态在黑暗条件下立即转换回Ni-A态。这些结果表明,光照对[NiFe]氢化酶Ni- a态的Fe位点的配位结构有明显的扰动,但Ni位点的配位变化相对较小。
[NiFe] hydrogenase catalyzes reversible oxidation of molecular hydrogen. Its active site is constructed of a hetero dinuclear Ni–Fe complex, and the oxidation state of the Ni ion changes according to the redox state of the enzyme. We found that the Ni-A state (an inactive unready, oxidized state) of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F (DvMF) is light sensitive and forms a new state (Ni-AL) with irradiation of visible light. The Fourier transform infrared (FT-IR) bands at 1956, 2084 and 2094cm−1of the Ni-A state shifted to 1971, 2086 and 2098cm−1in the Ni-AL state. The g-values of gx=2.30, gy=2.23 and gz=2.01 for the signals in the electron paramagnetic resonance (EPR) spectrum of the Ni-A state at room temperature varied for −0.009, +0.012 and +0.010, respectively, upon light irradiation. The light-induced Ni-AL state converted back immediately to the Ni-A state under dark condition at room temperature. These results show that the coordination structure of the Fe site of the Ni-A state of [NiFe] hydrogenase is perturbed significantly by light irradiation with relatively small coordination change at the Ni site.
DOI: 10.1016/j.str.2005.07.018
发表时间: 2005-11-01
期刊: STRUCTURE
影响因子: 5.7
作者:
Ogata, H;Hirota, S;Higuchi, Y
通讯作者: Higuchi, Y