ArticleBiochemistry2013
Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- A Metabolic Paradigm for Hydrogen Sulfide SignalingAntioxidants & redox signaling · 2023Review
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- Human Cystathionine γ-Lyase Is Inhibited byAntioxidants (Basel, Switzerland) · 2021Article
- Article
- Ferric heme as a CO/NO sensor in the nuclear receptor Rev-Erbß by coupling gas binding to electron transfer.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Role of endogenous and exogenous nitric oxide, carbon monoxide and hydrogen sulfide in HCT116 colon cancer cell proliferation.Biochemical pharmacology · 2018Article
- Allosteric control of human cystathionine β-synthase activity by a redox active disulfide bond.The Journal of biological chemistry · 2018Article
- Hydrogen Sulfide Biochemistry and Interplay with Other Gaseous Mediators in Mammalian Physiology.Oxidative medicine and cellular longevity · 2018Review
- Role of protein carbonylation in diabetes.Journal of inherited metabolic disease · 2018Review
- Beyond a Gasotransmitter: Hydrogen Sulfide and Polysulfide in Cardiovascular Health and Immune Response.Antioxidants & redox signaling · 2017Review
- A Clinically Relevant Variant of the Human Hydrogen Sulfide-Synthesizing Enzyme CystathionineOxidative medicine and cellular longevity · 2017Article
- Kinetics of Nitrite Reduction and Peroxynitrite Formation by Ferrous Heme in Human Cystathionine β-Synthase.The Journal of biological chemistry · 2016Article
- S-Adenosyl-l-methionine Modulates CO and NO• Binding to the Human H2S-generating Enzyme Cystathionine β-Synthase.The Journal of biological chemistry · 2016Article
- Hydrogen sulfide: physiological properties and therapeutic potential in ischaemia.British journal of pharmacology · 2015Review
- The therapeutic potential of cystathionine β-synthetase/hydrogen sulfide inhibition in cancer.Antioxidants & redox signaling · 2015Review
- S-glutathionylation enhances human cystathionine β-synthase activity under oxidative stress conditions.Antioxidants & redox signaling · 2015Article
- Alternative functions of the brain transsulfuration pathway represent an underappreciated aspect of brain redox biochemistry with significant potential for therapeutic engagement.Free radical biology & medicine · 2015Review
- Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part II. Pathophysiological and therapeutic aspects.British journal of pharmacology · 2014Review
- NO* binds human cystathionine β-synthase quickly and tightly.The Journal of biological chemistry · 2014Article
- Nitrite reductase activity and inhibition of H₂S biogenesis by human cystathionine ß-synthase.PloS one · 2014Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Cystathionine β-synthase (CBS) catalyzes the condensation of homocysteine with serine or cysteine to form cystathionine and water or hydrogen sulfide (H2S), respectively. In addition to pyridoxal phosphate, human CBS has a heme cofactor with cysteine and histidine as ligands. While Fe(III)-CBS is inert to exogenous ligands, Fe(II)-CBS can be reversibly inhibited by carbon monoxide (CO) and reoxidized by O2 to yield superoxide radical. In this study, we have examined the kinetics of Fe(II)CO-CBS formation and reoxidation. Reduction of Fe(III)-CBS by dithionite showed a square root dependence on concentration, indicating that the reductant species was the sulfur dioxide radical anion (SO2(•-)) that exists in rapid equilibrium with S2O4(2-). Formation of Fe(II)CO-CBS from Fe(II)-CBS and 1 mM CO occurred with a rate constant of (3.1 ± 0.4) × 10(-3) s(-1) (pH 7.4, 25 °C). The reaction of Fe(III)-CBS with the reduced form of the flavoprotein methionine synthase reductase in the presence of CO and NADPH resulted in its reduction and carbonylation to form Fe(II)CO-CBS. Fe(II)-CBS was formed as an intermediate with a rate constant of (9.3 ± 2.5) × 10(2) M(-1) s(-1). Reoxidation of Fe(II)CO-CBS by O2 was multiphasic. The major phase showed a hyperbolic dependence on O2 concentration. Although H2S is a product of the CBS reaction and a potential heme ligand, we did not find evidence of an effect of exogenous H2S on activity or heme binding. Reversible reduction of CBS by a physiologically relevant oxidoreductase is consistent with a regulatory role for the heme and could constitute a mechanism for cross talk among the CO, H2S, and superoxide signaling pathways.
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