Eggen R I, van Kranenburg R, Vriesema A J, Geerling A C, Verhagen M F, Hagen W R, de Vos W M
Department of Microbiology, Wageningen Agricultural University, Wageningen 6703 CT, The Netherlands.
J Biol Chem. 1996 Jun 14;271(24):14256-63. doi: 10.1074/jbc.271.24.14256.
Carbon monoxide dehydrogenase (Cdh) has been anaerobically purified from Methanosarcina frisia Gö1. The enzyme is a Ni2+-, Fe2+-, and S2--containing alpha2beta2 heterotetramer of 214 kDa with a pI of 5.2 and subunits of 94 and 19 kDa. It has a Vmax of 0.3 mmol of CO min-1 mg-1 and Km values for CO and methyl viologen of approximately 0.9 mM and 0.12 mM, respectively. EPR spectroscopy on the reduced enzyme showed two overlapping signals: one indicative for 2 (4Fe-4S)+ clusters and a second signal that is atypical for standard Fe/S clusters. The latter was, together with high-spin EPR signals of the oxidized enzyme tentatively assigned to an Fe/S cluster of high nuclearity.
一氧化碳脱氢酶（Cdh）已从弗里西亚甲烷八叠球菌Gö1中通过厌氧方式纯化得到。该酶是一种含Ni2+、Fe2+和S2-的α2β2异源四聚体，分子量为214 kDa，pI为5.2，亚基分子量分别为94 kDa和19 kDa。它的Vmax为0.3 mmol CO min-1 mg-1，对CO和甲基紫精的Km值分别约为0.9 mM和0.12 mM。对还原态酶进行的电子顺磁共振（EPR）光谱显示出两个重叠信号：一个指示2个（4Fe-4S）+簇，另一个信号对于标准铁硫簇来说是非典型的。后者与氧化态酶的高自旋EPR信号一起，初步被归属于一个高核的铁硫簇。
