{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,12]],"date-time":"2026-03-12T05:01:16Z","timestamp":1773291676513,"version":"3.50.1"},"reference-count":51,"publisher":"Wiley","issue":"22","license":[{"start":{"date-parts":[[2004,11,19]],"date-time":"2004-11-19T00:00:00Z","timestamp":1100822400000},"content-version":"vor","delay-in-days":18,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[2004,11]]},"abstract":"<jats:p>Heme oxygenase (HO) catalyzes the oxidative degradation of heme utilizing molecular oxygen and reducing equivalents. In photosynthetic organisms, HO functions in the biosynthesis of such open\u2010chain tetrapyrroles as phyto\u2010chromobilin and phycobilins, which are involved in the signal transduction for light responses and light harvesting for photosynthesis, respectively. We have determined the first crystal structure of a HO\u20101 from a photosynthetic organism, <jats:italic>Synechocystis<\/jats:italic> sp. PCC 6803 (Syn HO\u20101), in complex with heme at 2.5\u2003\u00c5 resolution. Heme\u2013Syn HO\u20101 shares a common folding with other heme\u2013HOs. Although the heme pocket of heme\u2013Syn HO\u20101 is, for the most part, similar to that of mammalian HO\u20101, they differ in such features as the flexibility of the distal helix and hydrophobicity. In addition, 2\u2010propanol derived from the crystallization solution occupied the hydrophobic cavity, which is proposed to be a CO trapping site in rat HO\u20101 that suppresses product inhibition. Although Syn HO\u20101 and mammalian HO\u20101 are similar in overall structure and amino acid sequence (57% similarity vs. human HO\u20101), their molecular surfaces differ in charge distribution. The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO\u20101 is narrow compared to that of mammalian HO\u20101. This feature is suited to the selective binding of ferredoxin, the physiological redox partner of Syn HO\u20101; the molecular size of ferredoxin is \u2248\u200a10\u2003kDa whereas the size of NADPH\u2010cytochrome P450 reductase, a reducing partner of mammalian HO\u20101, is \u2248\u200a77\u2003kDa. A docking model of heme\u2013Syn HO\u20101 and ferredoxin suggests indirect electron transfer from an iron\u2013sulfur cluster in ferredoxin to the heme iron of heme\u2013Syn HO\u20101.<\/jats:p>","DOI":"10.1111\/j.1432-1033.2004.04411.x","type":"journal-article","created":{"date-parts":[[2004,11,19]],"date-time":"2004-11-19T10:07:38Z","timestamp":1100858858000},"page":"4517-4525","source":"Crossref","is-referenced-by-count":49,"title":["Crystal structure of heme oxygenase\u20101 from cyanobacterium <i>Synechocystis<\/i> sp. 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