ArticleJournal of the American Chemical Society2009
The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 97 citations in OpenAlex.
- Article
- Engineering neuroglobin nitrite reductase activity based on myoglobin models.Biochemistry and biophysics reports · 2023Article
- Reversible thermally induced spin crossover in the myoglobin-nitrito adduct directly monitored by resonance Raman spectroscopy.RSC advances · 2023Article
- NMR-guided directed evolution.Nature · 2022Article
- Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations.Nitric oxide : biology and chemistry · 2022Article
- Intracellular imaging of metmyoglobin and oxygen using new dual purpose probe EYFP-Myoglobin-mCherry.Journal of biophotonics · 2022Article
- Endogenous Hemoprotein-Dependent Signaling Pathways of Nitric Oxide and Nitrite.Inorganic chemistry · 2021Review
- Influence of the heme distal pocket on nitrite binding orientation and reactivity in Sperm Whale myoglobin.The Biochemical journal · 2021Article
- Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Nitrite and nitrate chemical biology and signalling.British journal of pharmacology · 2019Review
- Article
- Distinguishing Nitro vs Nitrito Coordination in Cytochrome c' Using Vibrational Spectroscopy and Density Functional Theory.Inorganic chemistry · 2017Article
- Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferrihemeChemical science · 2016Article
- Residues in the Distal Heme Pocket of Arabidopsis Non-Symbiotic Hemoglobins: Implication for Nitrite Reductase Activity.International journal of molecular sciences · 2016Article
- Synthetic heme/copper assemblies: toward an understanding of cytochrome c oxidase interactions with dioxygen and nitrogen oxides.Accounts of chemical research · 2015Article
- Exploring the mechanisms of the reductase activity of neuroglobin by site-directed mutagenesis of the heme distal pocket.Biochemistry · 2015Article
- Evaluating the capacity to generate and preserve nitric oxide bioactivity in highly purified earthworm erythrocruorin: a giant polymeric hemoglobin with potential blood substitute properties.The Journal of biological chemistry · 2015Article
- Nitric oxide generation from heme/copper assembly mediated nitrite reductase activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Generating S-nitrosothiols from hemoglobin: mechanisms, conformational dependence, and physiological relevance.The Journal of biological chemistry · 2013Article
- Heme/copper assembly mediated nitrite and nitric oxide interconversion.Journal of the American Chemical Society · 2012Article
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5 authors at 2 institutions in 1 country.
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Abstract
It is now well-established that mammalian heme proteins are reactive with various nitrogen oxide species and that these reactions may play significant roles in mammalian physiology. For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nitrite (NO(2)(-)) to nitric oxide (NO) under hypoxic conditions. We demonstrate here that the distal pocket histidine residue (His64) of horse heart metMb(III) (i.e., ferric Mb(III)) has marked effects on the mode of nitrite ion coordination to the iron center. X-ray crystal structures were determined for the mutant proteins metMb(III) H64V (2.0 A resolution) and its nitrite ion adduct metMb(III) H64V-nitrite (1.95 A resolution), and metMb(III) H64V/V67R (1.9 A resolution) and its nitrite ion adduct metMb(III) H64V/V67R-nitrite (2.0 A resolution). These are compared to the known structures of wild-type (wt) hh metMb(III) and its nitrite ion adduct hh metMb(III)-nitrite, which binds NO(2)(-) via an O-atom in a trans-FeONO configuration. Unlike wt metMb(III), no axial H(2)O is evident in either of the metMb(III) mutant structures. In the ferric H64V-nitrite structure, replacement of the distal His residue with Val alters the binding mode of nitrite from the nitrito (O-binding) form in the wild-type protein to a weakly bound nitro (N-binding) form. Reintroducing a H-bonding residue in the H64V/V67R double mutant restores the O-binding mode of nitrite. We have also examined the effects of these mutations on reactivities of the metMb(III)s with cysteine as a reducing agent and of the (ferrous) Mb(II)s with nitrite ion under anaerobic conditions. The Mb(II)s were generated by reduction of the Mb(III) precursors in a second-order reaction with cysteine, the rate constants for this step following the order H64V/V67R > H64V >> wt. The rate constants for the oxidation of the Mb(II)s by nitrite (giving NO as the other product) follow the order wt > H64V/V67R >> H64V and suggest a significant role of the distal pocket H-bonding residue in nitrite reduction.
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