Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
Proteins. 2012 Dec;80(12):2799-803. doi: 10.1002/prot.24177. Epub 2012 Sep 29.
NirD is part of the nitrite reductase complex NirBD that catalyses the reduction of nitrite to NH(3) in nitrate assimilation and anaerobic respiration. The crystal structure analysis of NirD from Mycobacterium tuberculosis shows a double β-sandwich fold. NirD is related in three-dimensional structure and sequence to the Rieske proteins; however, it does not contain any Fe-S cluster or other cofactors that might be involved in electron transfer. A cysteine residue at the protein surface, conserved in NirD homologues lacking the iron-sulfur cluster might be important for the interaction with NirB and possibly stabilize one of the Fe-S centers in this subunit.
NirD 是亚硝酸盐还原酶复合物 NirBD 的一部分,该复合物催化硝酸盐同化和无氧呼吸中亚硝酸盐向 NH(3) 的还原。结核分枝杆菌 NirD 的晶体结构分析表明其具有双β-夹心折叠。NirD 在三维结构和序列上与 Rieske 蛋白有关;然而,它不包含任何可能参与电子转移的 Fe-S 簇或其他辅因子。蛋白质表面的一个半胱氨酸残基,在缺乏铁硫簇的 NirD 同源物中保守,可能对与 NirB 的相互作用很重要,并可能稳定该亚基中的一个 Fe-S 中心。