2002
DOI: 10.1016/s0301-4622(02)00094-7
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The interplay between heme iron and protein sulfhydryls in the reaction of dimeric Scapharca inaequivalvis hemoglobin with nitric oxide

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Cited by 22 publications
(39 citation statements)
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“…As reported above, the low reactivity of Mt-trHbO reflects the unfavorable ligand accessibility to the heme distal pocket [18]. Unexpectedly, the very low value of l on for the reductive nitrosylation of penta-coordinated Scapharca inaequivalvis HbI may reflect either the non-occurrence of the heme-Fe(III)-NO intermediate or the concomitant nitrosation of the Cys92 residue affecting the heme-Fe reactivity [38]. On the other hand, the reactivity of ferric hexa-coordinated Glycine max Lb, horse cytochrome c , and rabbit HPX-heme-Fe ([37], [39], [40], [72] and present study) reflects the hexa- to penta-coordination conversion of the heme-Fe atom ([59], [65], [73] and present study) (Table 4).…”
Section: Resultsmentioning
confidence: 86%
“…As reported above, the low reactivity of Mt-trHbO reflects the unfavorable ligand accessibility to the heme distal pocket [18]. Unexpectedly, the very low value of l on for the reductive nitrosylation of penta-coordinated Scapharca inaequivalvis HbI may reflect either the non-occurrence of the heme-Fe(III)-NO intermediate or the concomitant nitrosation of the Cys92 residue affecting the heme-Fe reactivity [38]. On the other hand, the reactivity of ferric hexa-coordinated Glycine max Lb, horse cytochrome c , and rabbit HPX-heme-Fe ([37], [39], [40], [72] and present study) reflects the hexa- to penta-coordination conversion of the heme-Fe atom ([59], [65], [73] and present study) (Table 4).…”
Section: Resultsmentioning
confidence: 86%
“…Values of k on for reductive nitrosylation of HPX–heme(III), horse cytochrome c (III) [31,36] and human Ngb(III) [32] are lower than those reported for G. max Lb(III) [30], sperm whale Mb(III) [31,36], S. inaequivalvis HbI(III) [33] and human Hb(III) [31], possibly reflecting heme–Fe(III) atom hexa‐coordination [16,37, 38] (Table 1). Values of k off for NO dissociation from the heme(III)–NO proteins considered range between < 1 × 10 −4 and 1.4 × 10 1 s −1 (Table 1), reflecting the different stability of the heme–Fe(III)–NO complexes [30–33,36].…”
Section: Resultsmentioning
confidence: 99%
“…In all three mechanisms, the reductant is the exogenous NO, which is oxidized to either a nitrite or a nitrosonium ion (NO ϩ ). In a recent study, NO-induced autoreduction was observed in hemoglobin from a clam, Scapharca inaequivalvis (37). In that work, a 6C NO-bound ferrous species was observed instantaneously following the addition of NO to the ferric species.…”
Section: His-fementioning
confidence: 87%
“…NO-mediated conversion of a 6C NO-bound ferric protein to a 6C NO-bound ferrous protein has been well documented for histidineligated heme proteins such as hemoglobin and myoglobin (35)(36)(37). In these cases, exposure of the ferric protein to NO first produces a 6C NO-bound ferric heme via displacement of the distal water ligand by NO (Equation 2).…”
Section: Discussionmentioning
confidence: 99%