Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling

2011 ◽  
Vol 39 (6) ◽  
pp. 1864-1870 ◽  
Author(s):  
Jörg Simon ◽  
Melanie Kern ◽  
Bianca Hermann ◽  
Oliver Einsle ◽  
Julea N. Butt

Bacterial MCCs (multihaem cytochromes c) represent widespread respiratory electron-transfer proteins. In addition, some of them convert substrates such as nitrite, hydroxylamine, nitric oxide, hydrazine, sulfite, thiosulfate or hydrogen peroxide. In many cases, only a single function is assigned to a specific MCC in database entries despite the fact that an MCC may accept various substrates, thus making it a multifunctional catalyst that can play diverse physiological roles in bacterial respiration, detoxification and stress defence mechanisms. The present article briefly reviews the structure, function and biogenesis of selected MCCs that catalyse key reactions in the biogeochemical nitrogen and sulfur cycles.

2013 ◽  
Vol 31 (3) ◽  
pp. 278
Author(s):  
Wen-Qi XIE ◽  
Jin-Ping ZHANG ◽  
Jian-Yi TAN ◽  
Xiao-Li XUAN ◽  
Yong-Fei WANG ◽  
...  

1999 ◽  
Vol 344 (3) ◽  
pp. 643 ◽  
Author(s):  
Claire LE GOFFE ◽  
Geneviève VALLETTE ◽  
Anne JARRY ◽  
Chantal BOU-HANNA ◽  
Christian L. LABOISSE

2002 ◽  
Vol 53 (372) ◽  
pp. 1237-1247 ◽  
Author(s):  
Steven J. Neill ◽  
Radhika Desikan ◽  
Andrew Clarke ◽  
Roger D. Hurst ◽  
John T. Hancock

2010 ◽  
Vol 2010 ◽  
pp. 1-4 ◽  
Author(s):  
Heather J. Montgomery ◽  
Andrea L. Dupont ◽  
Hilary E. Leivo ◽  
J. Guy Guillemette

The nitric oxide synthase-like protein fromBacillus cereus(bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine andNG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation ofNG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.


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