2008
DOI: 10.1016/j.jinorgbio.2008.02.008
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Isolation, purification and characterization of hemerythrin from Methylococcus capsulatus (Bath)

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Cited by 41 publications
(36 citation statements)
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“…2A). These features are reminiscent of the methemerythrin spectrum attributed to a μ-oxo bridged diferric metallocenter (22). Addition of sodium dithionite to oxidized UreA2B2 under anaerobic conditions caused bleaching of the spectrum, in parallel to the restoration of activity, consistent with direct reduction of the active site ferric ions (Fig.…”
Section: Effects Of Medium Supplementation With Metal Ions On Urea2b2mentioning
confidence: 74%
“…2A). These features are reminiscent of the methemerythrin spectrum attributed to a μ-oxo bridged diferric metallocenter (22). Addition of sodium dithionite to oxidized UreA2B2 under anaerobic conditions caused bleaching of the spectrum, in parallel to the restoration of activity, consistent with direct reduction of the active site ferric ions (Fig.…”
Section: Effects Of Medium Supplementation With Metal Ions On Urea2b2mentioning
confidence: 74%
“…The CLJU_c21940 flavoprotein has 60% identity to a C. acetobutylicum flavoprotein (CA_C2449) that has demonstrated oxidase activity and is reduced by NROR (see Table S4 in the supplemental material) (57). Hemerythrins are proteins that carry oxygen and/or convert oxygen to hydrogen peroxide (81,82). C. ljungdahlii also has an annotated superoxide dismutase (CLJU_c29780), but expression of the gene coding for it was low for both 8%-O 2 -exposed and anaerobically cultured cells (data not shown).…”
Section: Resultsmentioning
confidence: 99%
“…Hemerythrins are characterized by a non-heme di-iron core that is not only bridged by the carboxylate side chains of Asp and Glu residues but also is μ-oxo bridged (Fe III -O-Fe III ) in the oxidized form (Kao et al ., 2008). The iron atoms are liganded by histidine residues, which are all conserved in HerA (Supporting Information Fig.…”
Section: Resultsmentioning
confidence: 99%
“…7A) showed two major absorption bands at 336 nm and 374 nm and a weaker feature around 500 nm, which represent ligand-to-metal charge transfer transitions from the μ-oxo bridge to Fe(III) within the di-iron core. These spectral features are diagnostic of the met form of hemerythrins (Kao et al ., 2008) where a hydroxide is liganded to one of the Fe(III) centres. Reduction of the met protein by dithionite resulted in the bleaching of each of these peaks (Fig.…”
Section: Resultsmentioning
confidence: 99%
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