Publication date: 2017 Source:The Chemistry and Biology of Nitroxyl (HNO)
Author(s): M.R. Kumar, P.J. Farmer
HNO reacts with the ferrous states of many heme proteins such as myoglobin and hemoglobin to form stable HNO-Fe(II) adducts. Like the analogous O2 adducts, the HNO adducts are diamagnetic, but with a characteristic HNO resonance in 1H NMR c.15ppm that splits into doublets for H15NO adducts. As an illustration, we discuss HNO adducts of several heme-pocket mutants of myoglobin, hemoglobins, and related heme proteins. The 1H and 15N NMR resonances, obtained by HSQC experiments, are shown to differentiate subunits and isoforms of proteins within mixtures. NMR characterizations of these HNO adducts is a unique tool that is a sensitive to structural changes within the oxygen-binding cavity, which we suggest may help define modes of oxygen binding and activation in other heme enzymes.
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
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Biochemistry
DOI: 10.1021/acs.biochem.6b00427
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01273/20160203/images/medium/bi-2015-01273d_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01273
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Inorg Chem. 2013 Nov 4;
Authors: Kleingardner JG, Bowman SE, Bren KL
Abstract
The heme in cytochromes c undergoes a conserved out-of-plane distortion known as ruffling. For cytochromes c from the bacteria Hydrogenobacter thermophilus and Pseudomonas aeruginosa , NMR and EPR spectra have been shown to be sensitive to the...
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NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
Content Type Journal Article
Category NMR structure note
Pages 1-5
DOI 10.1007/s10858-012-9633-6
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Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of...
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Heme binding to rabbit hemopexin and its domain I, obtained by proteolytic cleavage of intact hemopexin, was studied by EPR, MCD and 1H-NMR spectroscopies. The data obtained support the proposal that the heme Fe(III) is coordinated by two...
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14 Spectroscopic NMR Characterizations of HNO Adducts of Ferrous Heme Proteins
Linear Mode
