Structural determinants for the formation of sulfhemeprotein complexes

Román-Morales, Elddie; Pietri, Ruth; Ramos-Santana, Brenda J.; Vinogradov, Serge N.; Lewis-Ballester, Ariel; López‐Garriga, Juan

doi:10.1016/j.bbrc.2010.08.068

Cited by 45 publications

(58 citation statements)

References 28 publications

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“…8B), formation of a sulfheme complex has not been detected. In contrast, sulf- heme formation has been observed in Hbs from M. decora and L. terrestris, which live in sulfide-free environments and also contain histidine at the ligand binding site (67,74,78). Similar to Riftia, these Hbs are large, consisting of 144 hemecontaining globin chains with an analogous quaternary structure.…”

Section: Hbs From the Worm Riftia Pachyptilamentioning

confidence: 79%

“…Sulfheme production was only observed in the HbI glutamine ? histidine mutant and in proteins having histidine in their heme active site, including human Hb and Mb and the giant Hbs from Macrobdella decora and Lumbricus terrestris (67). The 620 nm band is only observed after addition of H 2 S to the proteins and is assigned to the sulfheme derivative.…”

Section: Pietri Et Almentioning

confidence: 95%

“…We also suggest that following heme reduction and in the presence of O 2 , proteins having a histidine residue in their heme environment can promote sulfheme formation. In fact, we have recently evaluated the role of histidine in sulfheme formation by introducing point mutations in the L. pectinata HbI heme pocket to mimic the distal site of Mb and to identify the residues involved in sulfheme formation (67). Formation of the sulfheme product was monitored by the characteristic 620 nm band and by resonance Raman spectroscopy.…”

Section: Pietri Et Almentioning

confidence: 99%

See 2 more Smart Citations

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Pietri

Román-Morales

López‐Garriga

2011

Antioxidants & Redox Signaling

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196

136

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Historically, hydrogen sulfide (H(2)S) has been regarded as a poisonous gas, with a wide spectrum of toxic effects. However, like ·NO and CO, H(2)S is now referred to as a signaling gas involved in numerous physiological processes. The list of reports highlighting the physiological effects of H(2)S is rapidly expanding and several drug candidates are now being developed. As with ·NO and CO, not a single H(2)S target responsible for all the biological effects has been found till now. Nevertheless, it has been suggested that H(2)S can bind to hemeproteins, inducing different responses that can mediate its effects. For instance, the interaction of H(2)S with cytochrome c oxidase has been associated with the activation of the ATP-sensitive potassium channels, regulating muscle relaxation. Inhibition of cytochrome c oxidase by H(2)S has also been related to inducing a hibernation-like state. Although H(2)S might induce these effects by interacting with hemeproteins, the mechanisms underlying these interactions are obscure. Therefore, in this review we discuss the current state of knowledge about the interaction of H(2)S with vertebrate and invertebrate hemeproteins and postulate a generalized mechanism. Our goal is to stimulate further research aimed at evaluating plausible mechanisms that explain H(2)S reactivity with hemeproteins.

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Section: Hbs From the Worm Riftia Pachyptilamentioning

confidence: 79%

Section: Pietri Et Almentioning

confidence: 95%

Section: Pietri Et Almentioning

confidence: 99%

See 1 more Smart Citation

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Pietri

Román-Morales

López‐Garriga

2011

Antioxidants & Redox Signaling

Self Cite

196

136

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“…However, at higher concentrations, H 2 S can react with oxyglobins to form sulfheme derivatives, which have weak affinities for O 2 [319, 321]. Formation of the sulfheme complex requires the presence of a histidine residue at the distal site [322, 323]. At physiological concentrations, the interactions of H 2 S with hemeproteins such as cytochrome c oxidase, myoglobin and hemoglobin are suggested to be associated with activation of ATP-sensitive potassium channels and regulation of muscle relaxation [320, 324, 325].…”

Section: The Chemical Biology Of H2smentioning

confidence: 99%

Biological signaling by small inorganic molecules

Basudhar

Ridnour

Cheng

et al. 2016

Coordination Chemistry Reviews

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Small redox active molecules such as reactive nitrogen and oxygen species and hydrogen sulfide have emerged as important biological mediators that are involved in various physiological and pathophysiological processes. Advancement in understanding of cellular mechanisms that tightly regulate both generation and reactivity of these molecules is central to improved management of various disease states including cancer and cardiovascular dysfunction. Imbalance in the production of redox active molecules can lead to damage of critical cellular components such as cell membranes, proteins and DNA and thus may trigger the onset of disease. These small inorganic molecules react independently as well as in a concerted manner to mediate physiological responses. This review provides a general overview of the redox biology of these key molecules, their diverse chemistry relevant to physiological processes and their interrelated nature in cellular signaling.

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“…The reaction of H 2 S with hemoglobin and myoglobin to produce sulfheme derivatives has been extensively investigated and results in the covalent addition of sulfide to one of the pyrrole rings. 7 Sulfheme formation has also been noted during the catalytic cycle of lactoperoxidase 8 and catalase. 9 …”

Section: Introductionmentioning

confidence: 97%

Hydrogen Sulfide Oxidation by Myoglobin

et al. 2016

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Enzymes in the sulfur network generate the signaling molecule, hydrogen sulfide (H2S), from the amino acids cysteine and homocysteine. Since it is toxic at elevated concentrations, cells are equipped to clear H2S. A canonical sulfide oxidation pathway operates in mitochondria, converting H2S to thiosulfate and sulfate. We have recently discovered the ability of ferric hemoglobin to oxidize sulfide to thiosulfate and iron-bound hydropolysulfides. In this study, we report that myoglobin exhibits a similar capacity for sulfide oxidation. We have trapped and characterized iron-bound sulfur intermediates using cryo-mass spectrometry and X-ray absorption spectroscopy. Further support for the postulated intermediates in the chemically challenging conversion of H2S to thiosulfate and iron-bound catenated sulfur products is provided by EPR and resonance Raman spectroscopy in addition to density functional theory computational results. We speculate that the unusual sensitivity of skeletal muscle cytochrome c oxidase to sulfide poisoning in ethylmalonic encephalopathy, resulting from the deficiency in a mitochondrial sulfide oxidation enzyme, might be due to the concentration of H2S by myoglobin in this tissue.

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Structural determinants for the formation of sulfhemeprotein complexes

Cited by 45 publications

References 28 publications

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Biological signaling by small inorganic molecules

Hydrogen Sulfide Oxidation by Myoglobin

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