来自电子顺磁共振光谱法的关于巨大脱硫弧菌铁钼蛋白（醛氧化还原酶）中铁硫中心的信息。
Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas.
作者信息
Bray R C, Turner N A, Le Gall J, Barata B A, Moura J J
机构信息
School of Biological Sciences, University of Sussex, Brighton, U.K.
出版信息
Biochem J. 1991 Dec 15;280 ( Pt 3)(Pt 3):817-20. doi: 10.1042/bj2800817.
Abstract
E.p.r. spectra of reduced iron-sulphur centres of the aldehyde oxidoreductase (iron-molybdenum protein) of Desulfovibrio gigas were recorded at X-band and Q-band frequencies and simulated. Results are consistent with the view that only two types of [2Fe-2S] clusters are present, as in eukaryotic molybdenum-containing hydroxylases. The data indicate the Fe/SI centre to be very similar, and the Fe/SII centre somewhat similar, to these centres in the eukaryotic enzymes.
摘要
在X波段和Q波段频率下记录并模拟了巨大脱硫弧菌醛氧化还原酶（铁钼蛋白）的还原态铁硫中心的电子顺磁共振（E.p.r.）光谱。结果与如下观点一致：与真核含钼羟化酶一样，仅存在两种类型的[2Fe-2S]簇。数据表明，Fe/SI中心与真核酶中的这些中心非常相似，Fe/SII中心与真核酶中的这些中心有些相似。
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