Siroheme

Structure of siroheme

Siroheme (or sirohaem) is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen.[1] It is a cofactor at the active site of sulfite reductase, which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide, which can be incorporated into the organic compound homocysteine.[2]

  1. ^ Matthew J. Murphy; et al. (1974). "Siroheme: A New Prosthetic Group Participating in Six-Electron Reduction Reactions Catalyzed by Both Sulfite and Nitrite Reductases". PNAS. 71 (3): 612–616. Bibcode:1974PNAS...71..612M. doi:10.1073/pnas.71.3.612. PMC 388061. PMID 4595566.
  2. ^ Dominique Thomas; Yolande Surdin-Kerjan (1997). "Metabolism of sulfur amino acids in Saccharomyces cerevisiae". Microbiology and Molecular Biology Reviews. 61 (4): 503–532. doi:10.1128/mmbr.61.4.503-532.1997. PMC 232622. PMID 9409150.