NDLI: Modulation of NO binding to cytochrome c' by distal and proximal haem pocket residues.

Please wait, while we are loading the content...

Ruthenium(III) dimethyl sulfoxide pyridinehydroxamic acid complexes as potential antimetastatic agents: synthesis, characterisation and in vitro pharmacological evaluation

Structural and spectroscopic studies of a model for catechol oxidase.

QM/MM theoretical study of the pentacoordinate Mn(III) and resting states of manganese-reconstituted cytochrome $P450_{cam}$

Mercury(II) complex formation with glutathione in alkaline aqueous solution

Inhibition of cathepsin B by Au(I) complexes: a kinetic and computational study.

Modulation of NO binding to cytochrome c' by distal and proximal haem pocket residues.

DNA cleavage and binding selectivity of a heterodinuclear Pt-Cu(3-Clip-Phen) complex.

Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants.

Ambidentate H-bonding by heme-bound NO: structural and spectral effects of -O versus -N H-bonding.

One of the possible mechanisms for the inhibition effect of Tb(III) on peroxidase activity in horseradish (Armoracia rusticana) treated with Tb(III).

Spectroscopic evidence for an all-ferrous [4Fe-4S]0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.

Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial complexes II and III and related proteins.

Year: 2008 Volume: 13 Issue: 3

Year: 2008 Volume: 13 Issue: 2

Year: 2008 Volume: 13 Issue: 1

Year: 2007 Volume: 12

Year: 2005 Volume: 10

Modulation of NO binding to cytochrome c' by distal and proximal haem pocket residues.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Barbieri, Sonia Murphy, Loretta M. Sawers, R. Gary Eady, Robert R. Hasnain, S. Samar
Description	Country affiliation: United kingdom Author Affiliation: Barbieri S ( Molecular Biophysics Group, STFC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK.)
Abstract	We have cloned and expressed the cycP gene encoding cytochrome c' from Alcaligenes xylosoxidans and generated mutations in Arg-124 and Phe-59, residues close to the haem, to probe their involvement in modulating the unusual spin-state equilibrium of the haem Fe and the unique proximal mode of binding of NO to form a stable five-coordinate adduct. Arg-124 is located in the proximal pocket of the haem and forms a hydrogen bond to the stable five-coordinated bound NO. Phe-59 provides steric hindrance at the distal face where NO binds initially to form a six-coordinate adduct. Optical spectroscopy showed altered electronic properties of the oxidised haem centre resulting from the mutations of both residues. The high affinity of the ferrous proteins for NO remained unchanged and all of the mutational variants formed a stable five-coordinate NO species (lambda(Soret) 395 nm) in the presence of stoichiometric concentrations of NO. However, the kinetics of the reactivity towards NO were altered, with mutation of the distal Phe-59 residue resulting in the transient six-coordinate distally bound NO adduct (lambda(Soret) 415 nm) not being detected. Surprisingly, substitution of the proximal residue Arg-124 with Phe, Ala, Gln or Glu also resulted in the six-coordinate adduct not being detected, showing that this proximal residue also modulates reactivity towards NO on the opposite haem face. In contrast, the R124L substitution retained the property of the native protein in the initial formation of a six-coordinate NO adduct, a finding of functional importance since a Lys or an Arg residue is invariant in these proteins.
File Format	HTM / HTML
ISSN	09498257
Issue Number	4
Volume Number	13
e-ISSN	14321327
Journal	JBIC Journal of Biological Inorganic Chemistry
Language	English
Publisher	Springer
Publisher Date	2008-05-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Cytochromes C' Chemistry Metabolism Heme Nitric Oxide Alcaligenes Enzymology Genetics Amino Acid Substitution Binding Sites Escherichia Coli Hydrogen-ion Concentration Models, Molecular Mutation Protein Structure, Tertiary Spectrophotometry Titrimetry Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Modulation of NO binding to cytochrome c′ by distal and proximal haem pocket residues

Modulation of ligand–heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond–second temporal range

Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli.

Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?

Gates and Binding Pockets for Nitric Oxide with Cytochrome c′, According to Molecular Dynamics

Apolar distal pocket mutants of yeast cytochrome c peroxidase: Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants.

Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli

Apolar Distal Pocket Mutants of Yeast Cytochrome c Peroxidase: Hydrogen Peroxide Reactivity and Cyanide Binding of the TriAla, TriVal, and TriLeu Variants

The heme groups of cytochrome o from Escherichia coli.

Modulation of NO binding to cytochrome c' by distal and proximal haem pocket residues.

Similar Documents

Modulation of NO binding to cytochrome c′ by distal and proximal haem pocket residues

Modulation of ligand–heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond–second temporal range

Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli.

Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?

Gates and Binding Pockets for Nitric Oxide with Cytochrome c′, According to Molecular Dynamics

Apolar distal pocket mutants of yeast cytochrome c peroxidase: Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to the triAla, triVal, and triLeu variants.

Heme/heme redox interaction and resolution of individual optical absorption spectra of the hemes in cytochrome bd from Escherichia coli

Apolar Distal Pocket Mutants of Yeast Cytochrome c Peroxidase: Hydrogen Peroxide Reactivity and Cyanide Binding of the TriAla, TriVal, and TriLeu Variants

The heme groups of cytochrome o from Escherichia coli.

Modulation of NO binding to cytochrome c' by distal and proximal haem pocket residues.