Kurtz Donald M, Coulter Eric D
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens 30602-2556, USA.
J Biol Inorg Chem. 2002 Jun;7(6):653-8. doi: 10.1007/s00775-002-0360-4. Epub 2002 Apr 5.
Exposure of obligately anaerobic bacteria and archaea to transiently aerobic or micro-aerobic growth habitats requires that these microorganisms protect against oxidative stress resulting from adventitious dioxygen reduction. Superoxide reductases (SORs), which catalyze reduction of superoxide to hydrogen peroxide, have been identified as one component of a novel oxidative stress protection system in anaerobic bacteria and archaea. SORs contain a unique non-heme [Fe(His)(4)(Cys)] active site. This Commentary addresses the mechanism of superoxide reduction catalyzed by this unique active site in SORs both in vitro and in vivo.
专性厌氧细菌和古菌暴露于短暂需氧或微需氧的生长环境中，这要求这些微生物抵御因偶然的双原子氧还原而产生的氧化应激。超氧化物还原酶（SORs）催化超氧化物还原为过氧化氢，已被确定为厌氧细菌和古菌中新型氧化应激保护系统的一个组成部分。SORs含有独特的非血红素[Fe(His)(4)(Cys)]活性位点。本述评探讨了该独特活性位点在体外和体内催化SORs超氧化物还原的机制。
