A Comparative Resonance Raman Analysis of Heme-Binding PAS Domains:  Heme Iron Coordination Structures of theBjFixL,AxPDEA1,EcDos, andMtDos Proteins†

Biochemistry ◽  
2002 ◽  
Vol 41 (15) ◽  
pp. 4819-4826 ◽  
Author(s):  
Takeshi Tomita ◽  
Gonzalo Gonzalez ◽  
Alan L. Chang ◽  
Masao Ikeda-Saito ◽  
Marie-Alda Gilles-Gonzalez
Keyword(s):  
Resonance Raman ◽  
Heme Iron ◽  
Heme Binding ◽  
Raman Analysis ◽  
Iron Coordination

scholarly journals A Comparative Resonance Raman Analysis of Heme-Binding PAS Domains:  Heme Iron Coordination Structures of theBjFixL,AxPDEA1,EcDos, andMtDos Proteins,

Biochemistry ◽  
2002 ◽  
Vol 41 (20) ◽  
pp. 6572-6572
Author(s):  
Takeshi Tomita ◽  
Gonzalo Gonzalez ◽  
Alan L. Chang ◽  
Masao Ikeda-Saito ◽  
Marie-Alda Gilles-Gonzalez
Keyword(s):  
Resonance Raman ◽  
Heme Iron ◽  
Heme Binding ◽  
Raman Analysis ◽  
Iron Coordination

scholarly journals Analysis of Heme Iron Coordination in DGCR8: The Heme-Binding Component of the Microprocessor Complex

Biochemistry ◽  
2016 ◽  
Vol 55 (36) ◽  
pp. 5073-5083 ◽  
Author(s):  
Hazel M. Girvan ◽  
Justin M. Bradley ◽  
Myles R. Cheesman ◽  
James R. Kincaid ◽  
Yilin Liu ◽  
...  
Keyword(s):  
Heme Iron ◽  
Heme Binding ◽  
Microprocessor Complex ◽  
Iron Coordination ◽  
Binding Component

Resonance Raman Analysis of the Tryptophan Cation Radical

2014 ◽  
Vol 5 (17) ◽  
pp. 3009-3014 ◽  
Author(s):  
Hannah S. Shafaat ◽  
Judy E. Kim
Keyword(s):  
Resonance Raman ◽  
Cation Radical ◽  
Raman Analysis

The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies

2004 ◽  
Vol 1703 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Milan Fedurco ◽  
Jan Augustynski ◽  
Chiara Indiani ◽  
Giulietta Smulevich ◽  
Marián Antalík ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Heme Iron ◽  
Electrochemical Studies ◽  
Iron Coordination

scholarly journals The Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein implicated in heme degradation

2020 ◽  
Vol 477 (24) ◽  
pp. 4785-4796
Author(s):  
Jia Wang ◽  
Qi Guo ◽  
Xiaoyi Li ◽  
Xiao Wang ◽  
Lin Liu
Keyword(s):  
Crystal Structure ◽  
Recombinant Protein ◽  
Water Molecule ◽  
Heme Oxygenase ◽  
Protein Complex ◽  
Biosynthetic Pathway ◽  
Initial Step ◽  
Heme Iron ◽  
Heme Binding ◽  
New Protein

Plant tetrapyrroles, including heme and bilins, are synthesized in plastids. Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to the linear tetrapyrrole biliverdin as the initial step in bilin biosynthesis. Besides the canonical α-helical HO that is conserved from prokaryotes to human, a subfamily of non-canonical dimeric β-barrel HO has been found in bacteria. In this work, we discovered that the Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein that is structurally related to the putative non-canonical HO and is located in chloroplasts. The recombinant protein was able to bind and degrade heme in a manner different from known HO proteins. Crystal structure of the heme–protein complex reveals that the heme-binding site is in the interdimer interface and the heme iron is co-ordinated by a fixed water molecule. Our results identify a new protein that may function additionally in the tetrapyrrole biosynthetic pathway.

scholarly journals The effects of nitrogen-heme-iron coordination on substrate affinities for cytochrome P450 2E1

2011 ◽  
Vol 193 (1) ◽  
pp. 50-56 ◽  
Author(s):  
Jeffrey P. Jones ◽  
Carolyn A. Joswig-Jones ◽  
Michelle Hebner ◽  
Yuzhuo Chu ◽  
Dennis R. Koop
Keyword(s):  
Cytochrome P450 ◽  
Heme Iron ◽  
Cytochrome P450 2E1 ◽  
Iron Coordination ◽  
Substrate Affinities

scholarly journals Resonance Raman Spectroscopy of Mn-Mgk Cation Complexes in GaN

Crystals ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 235 ◽  
Author(s):  
Andrii Nikolenko ◽  
Viktor Strelchuk ◽  
Bogdan Tsykaniuk ◽  
Dmytro Kysylychyn ◽  
Giulia Capuzzo ◽  
...  
Keyword(s):  
Relative Intensity ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Photonic Devices ◽  
Temperature Dependent ◽  
Raman Analysis ◽  
Electron Phonon Interaction ◽  
Resonance Enhancement ◽  
Resonance Process ◽  
Cation Complexes

Resonance Raman analysis is performed in order to gain insight into the nature of impurity-induced Raman features in GaN:(Mn,Mg) hosting Mn-Mgk cation complexes and representing a prospective strategic material for the realization of full-nitride photonic devices emitting in the infra-red. It is found that in contrast to the case of GaN:Mn, the resonance enhancement of Mn-induced modes at sub-band excitation in Mg co-doped samples is not observed at an excitation of 2.4 eV, but shifts to lower energies, an effect explained by a resonance process involving photoionization of a hole from the donor level of Mn to the valence band of GaN. Selective excitation within the resonance Raman conditions allows the structure of the main Mn-induced phonon band at ~670 cm−1 to be resolved into two distinct components, whose relative intensity varies with the Mg/Mn ratio and correlates with the concentration of different Mn-Mgk cation complexes. Moreover, from the relative intensity of the 2LO and 1LO Raman resonances at inter-band excitation energy, the Huang-Rhys parameter has been estimated and, consequently, the strength of the electron-phonon interaction, which is found to increase linearly with the Mg/Mn ratio. Selective temperature-dependent enhancement of the high-order multiphonon peaks is due to variation in resonance conditions of exciton-mediated outgoing resonance Raman scattering by detuning the band gap.

scholarly journals Nitrosative stress sensing inPorphyromonas gingivalis: structure of and heme binding by the transcriptional regulator HcpR

2019 ◽  
Vol 75 (4) ◽  
pp. 437-450 ◽  
Author(s):  
B. Ross Belvin ◽  
Faik N. Musayev ◽  
John Burgner ◽  
J. Neel Scarsdale ◽  
Carlos R. Escalante ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Nitrosative Stress ◽  
Gas Sensing ◽  
Anaerobic Bacteria ◽  
Heme Iron ◽  
Heme Binding ◽  
X Ray ◽  
X Ray Scattering ◽  
Stress Sensing ◽  
High Degree

Although the HcpR regulator plays a vital step in initiation of the nitrosative stress response in many Gram-negative anaerobic bacteria, the molecular mechanisms that it uses to mediate gas sensing are not well understood. Here, a 2.6 Å resolution crystal structure of the N-terminal sensing domain of the anaerobic periodontopathogenPorphyromonas gingivalisHcpR is presented. The protein has classical features of the regulators belonging to the FNR-CRP family and contains a hydrophobic pocket in its N-terminal sensing domain. It is shown that heme bound to HcpR exhibits heme iron as a hexacoordinate system in the absence of nitric oxide (NO) and that upon nitrosylation it transitions to a pentacoordinate system. Finally, small-angle X-ray scattering experiments on full-length HcpR reveal that the C-terminal DNA-binding domain of HcpR has a high degree of interdomain flexibility.

Resonance Raman analysis of charge-transfer reorganization energies in a covalent dicyanoethylene-aza-adamantane

1996 ◽  
Vol 258 (1-2) ◽  
pp. 87-93 ◽  
Author(s):  
David Lee Phillips ◽  
Ian R. Gould ◽  
J.W. Verhoeven ◽  
Dietrich Tittelbach-Helmrich ◽  
Anne B. Myers
Keyword(s):  
Charge Transfer ◽  
Resonance Raman ◽  
Raman Analysis ◽  
Reorganization Energies
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