{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T11:28:14Z","timestamp":1793878094947,"version":"4.7.0"},"reference-count":43,"publisher":"Wiley","issue":"23","license":[{"start":{"date-parts":[[2006,10,31]],"date-time":"2006-10-31T00:00:00Z","timestamp":1162252800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2006,12]]},"abstract":"<jats:p>Heme oxygenase converts heme into biliverdin, CO, and free iron. In plants, as well as in cyanobacteria, heme oxygenase plays a particular role in the biosynthesis of photoreceptive pigments, such as phytochromobilins and phycobilins, supplying biliverdin IX<jats:sub>\u03b1<\/jats:sub> as a direct synthetic resource. In this study, a higher plant heme oxygenase, GmHO\u20101, of <jats:italic>Glycine max<\/jats:italic> (soybean), was prepared to evaluate the molecular features of its heme complex, the enzymatic activity, and the mechanism of heme conversion. The similarity in the amino acid sequence between GmHO\u20101 and heme oxygenases from other biological species is low, and GmHO\u20101 binds heme with 1\u2003:\u20031 stoichiometry at His30; this position does not correspond to the proximal histidine of other heme oxygenases in their sequence alignments. The heme bound to GmHO\u20101, in the ferric high\u2010spin state, exhibits an acid\u2013base transition and is converted to biliverdin IX<jats:sub>\u03b1<\/jats:sub> in the presence of NADPH\/ferredoxin reductase\/ferredoxin, or ascorbate. During the heme conversion, an intermediate with an absorption maximum different from that of typical verdoheme\u2013heme oxygenase or CO\u2013verdoheme\u2013heme oxygenase complexes was observed and was extracted as a bis\u2010imidazole complex; it was identified as verdoheme. A myoglobin mutant, H64L, with high CO affinity trapped CO produced during the heme degradation. Thus, the mechanism of heme degradation by GmHO\u20101 appears to be similar to that of known heme oxygenases, despite the low sequence homology. The heme conversion by GmHO\u20101 is as fast as that by SynHO\u20101 in the presence of NADPH\/ferredoxin reductase\/ferredoxin, thereby suggesting that the latter is the physiologic electron\u2010donating system.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2006.05531.x","type":"journal-article","created":{"date-parts":[[2006,10,31]],"date-time":"2006-10-31T12:18:21Z","timestamp":1162297101000},"page":"5384-5399","source":"Crossref","is-referenced-by-count":23,"title":["Spectroscopic characterization of a higher plant heme oxygenase isoform\u20101 from <i>Glycine max<\/i> (soybean)\u2003\u2212coordination structure of the heme complex and catabolism of 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