Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I fromLucina pectinata

Silfa, Eilyn; Almeida, Maritza; Cerda, José F.; Wu, Shaoxiong; López‐Garriga, Juan

doi:10.1002/(sici)1520-6343(1998)4:5<311::aid-bspy3>3.0.co;2-t

Cited by 21 publications

(11 citation statements)

References 51 publications

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“…Sulfheme formation in Mb and the HbI GlnE7His mutant was also confirmed by evaluating the vinyl bands (vC=C) at ~1620 cm −1 [26,27], in the RR spectra of Mb, HbI and HbI GlnE7His, with and without H 2 O 2 and H 2 S, as shown in Figure 2B. The Figure clearly shows that in the absence of H 2 O 2 and H 2 S, the vinyl modes can be deconvoluted into two distinct bands at 1620 and 1626 cm −1 .…”

Section: Resultsmentioning

confidence: 94%

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Structural determinants for the formation of sulfhemeprotein complexes

Román-Morales

Pietri

Ramos-Santana

et al. 2010

Biochemical and Biophysical Research Communications

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Several hemoglobins were explored by UV-Vis and resonance Raman spectroscopy to define sulfheme complex formation. Evaluation of these proteins upon the reaction with H2O2 or O2 in the presence of H2S suggest: (a) the formation of the sulfheme derivate requires a HisE7 residue in the heme distal site with an adequate orientation to form an active ternary complex; (b) that the ternary complex intermediate involves the HisE7, the peroxo or ferryl species, and the H2S molecule. This moiety precedes and triggers the sulfheme formation.

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Section: Resultsmentioning

confidence: 94%

“…The development of these bands in the Mb and HbI GlnE7His spectra, and not in the HbI spectrum, indicates a distortion of the heme group due to the incorporation of the sulfur ring [25]. This suggestion is supported by the fact that the 1353 and 1390cm −1 , peaks have been related to the B 1g pyrrole deformation of chlorin hemes [25,27]. …”

Section: Resultsmentioning

confidence: 99%

Structural determinants for the formation of sulfhemeprotein complexes

Román-Morales

Pietri

Ramos-Santana

et al. 2010

Biochemical and Biophysical Research Communications

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“…HbI exhibits a high association constant (k on = 2.3 × 10 5 M −1 s −1 ) and an unusually low dissociation constant (k off = 0.22 × 10 −3 s −1 ) for H 2 S, 390 which suggests the stabilization of distal sulfide ligand by the active site. 391,395,396,398,400,401 In human Hb, a histidine residue hydrogen bonds with the iron-bound sulfide. The corresponding residue in HbI is a glutamine, which has a flexible side chain.…”

Section: Coordinated H 2 Smentioning

confidence: 98%

Chemical Biology of H₂S Signaling through Persulfidation

et al. 2017

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Signaling by HS is proposed to occur via persulfidation, a posttranslational modification of cysteine residues (RSH) to persulfides (RSSH). Persulfidation provides a framework for understanding the physiological and pharmacological effects of HS. Due to the inherent instability of persulfides, their chemistry is understudied. In this review, we discuss the biologically relevant chemistry of HS and the enzymatic routes for its production and oxidation. We cover the chemical biology of persulfides and the chemical probes for detecting them. We conclude by discussing the roles ascribed to protein persulfidation in cell signaling pathways.

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“…(149). The ferric oxidation state is further stabilized by the electron-withdrawing character of the out-of-plane heme vinyl group, facilitating H 2 S binding (253).…”

Section: B Sulfidementioning

confidence: 99%

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

Reeder

2010

Antioxidants & Redox Signaling

167

184

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Pentacoordinate respiratory hemoproteins such as hemoglobin and myoglobin have evolved to supply cells with oxygen. However, these respiratory heme proteins are also known to function as redox enzymes, reacting with compounds such as nitric oxide and peroxides. The recent discoveries of hexacoordinate hemoglobins in vertebrates and nonsymbiotic plants suggest that the redox activity of globins is inherent to the molecule. The uncontrolled formation of radical species resulting from such redox chemistry on respiratory hemoproteins can lead to oxidative damage and cellular toxicity. In this review, we examine the functions of various globins and the mechanisms by which these globins act as redox enzymes under physiologic conditions. Evidence that redox reactions also occur under disease conditions, leading to pathologic complications, also is examined, focusing on recent discoveries showing that the ferryl oxidation state of these hemoproteins is present in these disease states in vivo. In addition, we review the latest advances in the understanding of globin redox mechanisms and how they might affect cellular signaling pathways and how they might be controlled therapeutically or, in the case of hemoglobin-based blood substitutes, through rational design.

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Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I fromLucina pectinata

Cited by 21 publications

References 51 publications

Structural determinants for the formation of sulfhemeprotein complexes

Structural determinants for the formation of sulfhemeprotein complexes

Chemical Biology of H₂S Signaling through Persulfidation

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

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Orientation of the heme vinyl groups in the hydrogen sulfide-binding hemoglobin I fromLucina pectinata

Cited by 21 publications

References 51 publications

Structural determinants for the formation of sulfhemeprotein complexes

Structural determinants for the formation of sulfhemeprotein complexes

Chemical Biology of H2S Signaling through Persulfidation

The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms

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Product

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Chemical Biology of H₂S Signaling through Persulfidation