Browsing by Subject "heme"
Now showing items 1-16 of 16
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Article
Coupling of helix E-F motion with the O-nitrito and 2-nitrovinyl coordination in myoglobin
(2017)Myoglobin (Mb) is known to react slowly with nitirite to form the green pigment by NO2 − cordination to the heme Fe in the O-binding nitrito (O1[sbnd]N[dbnd]O2) mode and to the heme 2-vinyl position. Nitrite is a powerful ...
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Article
Detection of the His-heme Fe2+-NO species in the reduction of NO to N2O by ba3-oxidase from thermus thermophilus
(2005)Reaction pathways in the enzymatic formation and cleavage of the N-N and N-O bonds, respectively, are difficult to verify without the structure of the intermediates, but we now have such information on the heme a3 2+-NO ...
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Direct detection of Fe(IV)=O intermediates in the cytochrome aa3 oxidase from Paracoccus denitrificans[H2O2 reaction
(2003)We report the first evidence for the formation of the "607- and 580-nm forms" in the cytochrome oxidase aa3/H2O2 reaction without the involvement of tyrosine 280. The pKa of the 607-580-nm transition is 7.5. The 607-nm ...
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Fourier transform infrared (FTIR) and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus thermophilus
(2002)Fourier transform infrared (FTIR) and step-scan time-resolved FTIR difference spectra are reported for the [carbonmonoxy]cytochrome caa3 from Thermus thermophilus. A major C-O mode of heme a3 at 1958 cm-1 and two minor ...
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Nitrite coordination in myoglobin
(2017)The coordination of nitrite in myoglobin (Mb) has been characterized by resonance Raman spectroscopy and the frequencies of the nitrite bound to the heme Fe as well to the 2-vinyl have been computed by density functional ...
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Article
The origin of the Fe IV = O intermediates in cytochrome aa 3 oxidase
(2012)The dioxygen reduction mechanism in cytochrome oxidases relies on proton control of the electron transfer events that drive the process. Proton delivery and proton channels in the protein that are relevant to substrate ...
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Probing nitrite coordination in horseradish peroxidase by resonance Raman spectroscopy: Detection of two binding sites
(2017)Nitrite is a powerful oxidant that affects the activity of peroxidases towards various substrates and leads to heme macrocycle modifications in members of the peroxidase family, such as the horseradish peroxidase (HRP). ...
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Probing the nitrite and nitric oxide reductase activity of cbb3 oxidase: Resonance Raman detection of a six-coordinate ferrous heme-nitrosyl species in the binuclear b3/CuB center
(2015)In this work we report the first spectroscopic evidence demonstrating that cbb3 oxidase catalyzes the reduction of nitrite to nitrous oxide under reducing anaerobic conditions. The reaction proceeds through the formation ...
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The protein effect in the structure of two ferryl-oxo intermediates at the same oxidation level in the heme copper binuclear center of cytochrome c oxidase
(2013)Identification of the intermediates and determination of their structures in the reduction of dioxygen to water by cytochrome c oxidase (CcO) are particularly important to understanding both O2 activation and proton pumping ...
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Recognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopy
(2006)The determination of ligand binding properties is a key step in our understanding of gas sensing and discrimination by gas sensory proteins. HemAT is a newly discovered signal transducer heme protein that recognizes O 2 ...
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Resonance Raman detection of the Fe2+-C-N modes in heme-copper oxidases: A probe of the active site
(2004)Resonance Raman spectroscopy has been employed to investigate the reduced cyano complexes of cytochrome aa3 from bovine heart and Rhodobacter sphaeroides and of cytochrome bo3 from E. coli. In the aa 3-type oxidases, the ...
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Resonance Raman detection of the myoglobin nitrito heme Fe-O-N=O/2-nitrovinyl species: Implications for helix E-helix F interactions
(2015)The description of biological activity in heme proteins responsible for activating small molecules requires identification of ligand movement into the metal and non-metal binding sites. Mechanisms of nitrite reductase ...
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The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy
(2015)Members of the cytochrome c oxidase family exhibit nitrite reductase activity. In this work, we have characterized a ferrous heme a3-nitro species in ba3-oxidase by resonance Raman spectroscopy. This provides the first ...
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The structure of the hyponitrite species in a heme Fe-Cu binuclear center
(2007)NO laughing matter: The enzymatic production of laughing gas (N 2O) from two molecules of NO requires the formation of the N-N bond and the subsequent cleavage of the N-OH bond. Resonance Raman spectroscopic studies have ...
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Time-Resolved Resonance Raman and Time-Resolved Step-Scan FTIR Studies of Nitric Oxide Reductase from Paracoccus denitrificans: Comparison of the Heme b3-FeB Site to That of the Heme-CuB in Oxidases
(2003)Time-resolved resonance Raman (TR3) and time-resolved step-scan (TRS2) FTIR spectroscopies have been used to probe the structural dynamics at the heme b3 proximal and distal sites after carbon monoxide photolysis from fully ...
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Two ligand-binding sites in the O2-sensing signal transducer HemAT: Implications for ligand recognition/discrimination and signaling
(2006)We have identified a ligand (CO) accommodation cavity in the signal transducer sensor protein HemAT (heme-based aerotactic transducer) that allows us to gain single-molecule insights into the mechanism of gas sensor proteins. ...