肺炎克雷伯菌固氮酶铁钼辅因子的铁 K 边 X 射线吸收光谱
Iron K-edge X-ray absorption spectroscopy of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae.
作者信息
Arber J M, Flood A C, Garner C D, Gormal C A, Hasnain S S, Smith B E
机构信息
Department of Chemistry, University of Manchester, U.K.
出版信息
Biochem J. 1988 Jun 1;252(2):421-5. doi: 10.1042/bj2520421.
Abstract
Iron K-edge X-ray absorption data for the iron-molybdenum cofactor ('FeMoco') from Klebsiella pneumoniae reported here provide the first evidence for long-range structural order in the cofactor [Fe...Fe(Mo) = 0.368 nm in addition to Fe...S = 0.22 nm and Fe...Fe(Mo) = 0.27 nm] and, in contrast with previously published data [Antonio, Teo, Orme-Johnson, Nelson, Groh, Lindahl, Kauzlarich & Averill (1982) J. Am. Chem. Soc. 104, 4703-4705], indicate that most of the iron centres are not co-ordinated to light (oxygen, nitrogen) atoms. This demonstrates that presently available chemical models for FeMoco are inadequate.
摘要
本文报道的肺炎克雷伯氏菌铁钼辅因子（“FeMoco”）的铁K边X射线吸收数据首次证明了该辅因子中存在长程结构有序性[除了铁硫键长为0.22纳米和铁铁（钼）键长为0.27纳米外，铁铁（钼）键长为0.368纳米]，并且与之前发表的数据[安东尼奥、特奥、奥姆-约翰逊、尼尔森、格罗、林达尔、考兹拉里奇和埃弗里尔（1982年）《美国化学会志》104，4703 - 4705]相反，表明大多数铁中心并未与轻（氧、氮）原子配位。这表明目前可用的FeMoco化学模型并不充分。
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