Identification of the altered pyrrole in sulfmyoglobin and an extractable sulfhemin:  participation of the 4-vinyl group in the saturation of the pyrrole in one form of sulfmyoglobin

Chatfield, Mariann J.; Mar, Gerd N. La; Lecomte, Juliette T. J.; Balch, Alan L.; Smith, Kevin M.; Langry, Kevin C.

doi:10.1021/ja00282a048

Cited by 31 publications

(20 citation statements)

References 3 publications

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“…SCMb is the most stable of these derivatives and has been suggested by subsequent NMR studies to possess a prosthetic group with a structure similar to that shown in Fig. 1 (17)(18)(19). Additional NMR experiments have yielded a spatial configuration for the heme substituents that is consistent with this model and that predicts the absolute configuration of the resulting chiral center about carbon atom C2C (20).…”

supporting

confidence: 52%

Three-dimensional structure of cyanomet-sulfmyoglobin C.

Evans

Sishta²,

Mauk³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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The atomic structure of horse heart cyanomet-sulfmyoglobin C has been establied by x-ray crystalographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfnyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sufuratom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.

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supporting

confidence: 52%

Three-dimensional structure of cyanomet-sulfmyoglobin C.

Evans

Sishta²,

Mauk³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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“…Later, proton NMR studies of sulfMb identified the sulfur atom on pyrrole B by analyzing the chemical shifts of the heme 1,3,5,8-methyls and the 2,4-vinyl substitutions [31, 34, 47]. Based on NMR and resonance Raman data it was then proved that the sulfur atom is incorporated across the double β-β bond of pyrrole B either as episulfide or thiochlorin, with a heme-chlorin type structure [26, 28, 30, 31, 34, 44, 47, 48]. The band at 620 nm observed in the optical spectra of sulfHb and sulfMb reflects the nature of the chlorin structure.…”

Section: Interaction Of H2s With Myoglobin and Hemoglobinmentioning

confidence: 99%

“…Proton NMR studies of several sulfMbCN complexes revealed that there are at least three isomeric forms of the chlorin structure that may affects O 2 affinity [29, 30]. As shown in Figure 4b, each sulfheme isomer, named sulfMbA, sulfMbB and sulfMbC, have different chemical properties and hence, different reactivity and stability [29, 34].…”

Section: Interaction Of H2s With Myoglobin and Hemoglobinmentioning

confidence: 99%

“…SulfMbA is converted to both sulfMbB and sulfMbC, but conversion from sulfMbB to sulfMbC has not been observed, indicating that sulfMbA is the precursor of the other two sulfhemes species [28, 34]. SulfMbC is the most stable isomeric form and is only observed when the 4-vinyl is on heme [30, 52]. Replacing this vinyl group with hydrogen only yields sulfMbA and sulfMbB and two other red sulfMb isomers (D and E), which apparently forms from the former two isomers [52].…”

Section: Interaction Of H2s With Myoglobin and Hemoglobinmentioning

confidence: 99%

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Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Ríos-González¹,

Román-Morales²,

Pietri³

et al. 2014

Journal of Inorganic Biochemistry

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Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (•NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins. For example, interaction of H2S with the oxygenated form of human hemoglobin and myoglobin produces a sulfheme protein complex that has been implicated in H2S degradation. The presence of this sulfheme derivative has also been used as a marker for endogenous H2S synthesis and metabolism. Remarkably, human catalases and peroxidases also generate this sulfheme product. In this review, we describe the structural and functional aspects of the sulfheme derivative in these proteins and postulate a generalized mechanism for sulfheme protein formation. We also evaluate the possible physiological function of this complex and highlight the issues that remain to be assessed to determine the role of sulheme proteins in H2S metabolism, detection and physiology.

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“…1 B [lo]. Under basic conditions decay of SAMb yields mainly &Mb, the thermodynamically stable product [6,7,10], which has been shown to contain a chlorin prosthetic group in which the vinyl group of pyrole II has formed an exocyclic thiolene ring [8,9], Fig. 1C.…”

Section: Metmb + H202 + Ferrylmb Ferrylmb + Hs + Fe(iii)sulphmbmentioning

confidence: 99%

Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli

Lloyd

Mauk

1994

FEBS Letters

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Expression of recombinant horse heart myoglobin in Escherichia coli has been found to result in the production of both native and variable amounts (-1617% total) of two sulphmyoglobin isomers. The recombinant sulphmyoglobin produced consists primarily of the A and B isomers as identified by 'H NMR spectroscopy with no evidence for production of the C isomer. Conversion of recombinant sulphmyoglobin to the native protein can be achieved by reconstitution with protohaem IX. The possible relationship of this observation to recombinant expression of other heme proteins is discussed.

show abstract

Identification of the altered pyrrole in sulfmyoglobin and an extractable sulfhemin: participation of the 4-vinyl group in the saturation of the pyrrole in one form of sulfmyoglobin

Cited by 31 publications

References 3 publications

Three-dimensional structure of cyanomet-sulfmyoglobin C.

Three-dimensional structure of cyanomet-sulfmyoglobin C.

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli

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