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Cytochrome c'-beta from Methylococcus capsulatus (Bath) and similar proteins Cytochromes (cyt) c' are defined by a pentacoordinate heme Fe with a CXXCH c-heme-binding motif located close to the C-terminus. Most cyt c' have four alpha-helix bundle structures, and are referred to as cyt c'-alpha. M. capsulatus (Bath) cytochrome c'-beta, encoded by the cytS gene, is a homodimeric heme protein with a higher molecular weight of about 16 kDa per monomer, compared to cyt c'-alpha (~12 kDa), and it adopts a beta-sheet structure. It is involved in nitric oxide scavenging and protection against nitrosoative stress. Cyt c'-beta belongs to a family, called the cytochrome P460 family, of small mono-heme c-type cytochromes that are predominantly of beta-sheet structure, as opposed to the four elongate, tightly-packed alpha-helices of the widely distributed cytochromes c' of photoheterotrophic and denitrifying bacteria. |
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