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Wolinella succinogenes octaheme sulfite reductase MccA, form II
Structural highlights
FunctionMCCA_WOLSU Respiratory sulfite reductase that catalyzes the reduction of sulfite to sulfide in a single step, consuming six electrons in the process (PubMed:22040142, PubMed:25642962). Required for sulfite respiration under anaerobic growth conditions (PubMed:22040142). Has only marginal activity with nitrite.[1] [2] Publication Abstract from PubMedThe six-electron reduction of sulfite to sulfide is the pivot point of the biogeochemical cycle of the element sulfur. The octahaem cytochrome c MccA (also known as SirA) catalyses this reaction for dissimilatory sulfite utilization by various bacteria. It is distinct from known sulfite reductases because it has a substantially higher catalytic activity and a relatively low reactivity towards nitrite. The mechanistic reasons for the increased efficiency of MccA remain to be elucidated. Here we show that anoxically purified MccA exhibited a 2- to 5.5-fold higher specific sulfite reductase activity than the enzyme isolated under oxic conditions. We determined the three-dimensional structure of MccA to 2.2 A resolution by single-wavelength anomalous dispersion. We find a homotrimer with an unprecedented fold and haem arrangement, as well as a haem bound to a CX15CH motif. The heterobimetallic active-site haem 2 has a Cu(I) ion juxtaposed to a haem c at a Fe-Cu distance of 4.4 A. While the combination of metals is reminiscent of respiratory haem-copper oxidases, the oxidation-labile Cu(I) centre of MccA did not seem to undergo a redox transition during catalysis. Intact MccA tightly bound SO2 at haem 2, a dehydration product of the substrate sulfite that was partially turned over due to photoreduction by X-ray irradiation, yielding the reaction intermediate SO. Our data show the biometal copper in a new context and function and provide a chemical rationale for the comparatively high catalytic activity of MccA. The octahaem MccA is a haem c-copper sulfite reductase.,Hermann B, Kern M, La Pietra L, Simon J, Einsle O Nature. 2015 Feb 2. doi: 10.1038/nature14109. PMID:25642962[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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