普通脱硫弧菌氢化酶：一种不含镍的非血红素铁酶，其电子顺磁共振（EPR）和穆斯堡尔谱显示异常。
Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra.
作者信息
Huynh B H, Czechowski M H, Krüger H J, DerVartanian D V, Peck H D, LeGall J
出版信息
Proc Natl Acad Sci U S A. 1984 Jun;81(12):3728-32. doi: 10.1073/pnas.81.12.3728.
Abstract
A purification procedure for the periplasmic hydrogenase from Desulfovibrio vulgaris ( Hildenborough , National Collection of Industrial Bacteria 8303) is reported. The purified hydrogenase has a specific activity of 4800 units per mg of protein. Plasma emission studies reveal that this highly active hydrogenase is free of nickel and contains 11 (+/- 1) nonheme iron atoms per molecule. A combined EPR and Mössbauer study indicates that the majority of the iron atoms are bound in the form of iron- sulfur clusters. Two ferredoxin-type [4Fe-4S] clusters have been identified that exhibit normal EPR and Mössbauer parameters; however, no trace of 3Fe cluster is detected by the Mössbauer measurement. In the presence of oxidants, cytochrome c3, and CO, anomalous EPR and Mössbauer spectra indicative of atypical nonheme iron centers are observed.
摘要
本文报道了普通脱硫弧菌（希登伯勒，国家工业细菌收藏中心8303）周质氢化酶的纯化方法。纯化后的氢化酶比活性为每毫克蛋白质4800单位。等离子体发射研究表明，这种高活性氢化酶不含镍，每个分子含有11（±1）个非血红素铁原子。电子顺磁共振（EPR）和穆斯堡尔谱的联合研究表明大多数铁原子以铁硫簇的形式结合。已鉴定出两个铁氧化还原蛋白型[4Fe-4S]簇，它们具有正常的EPR和穆斯堡尔参数；然而，穆斯堡尔测量未检测到3Fe簇的痕迹。在氧化剂、细胞色素c3和CO存在的情况下，观察到指示非典型非血红素铁中心的异常EPR和穆斯堡尔谱。
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Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra.普通脱硫弧菌氢化酶：一种不含镍的非血红素铁酶，其电子顺磁共振（EPR）和穆斯堡尔谱显示异常。
Proc Natl Acad Sci U S A. 1984 Jun;81(12):3728-32. doi: 10.1073/pnas.81.12.3728.
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