NDLI: Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

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

Thermodynamics and molecular dynamics simulations of calcium binding to the regulatory site of human cardiac troponin C: evidence for communication with the structural calcium binding sites

Bis(thiosemicarbazone) copper complexes: mechanism of intracellular accumulation

Binding properties of Ru(II) polypyridyl complexes with poly(U)·poly(A)*poly(U) triplex: the ancillary ligand effect on third-strand stabilization

Synthesis and structural characterization of soluble neuromelanin analogs provides important clues to its biosynthesis

Fe–O versus O–O bond cleavage in reactive iron peroxide intermediates of superoxide reductase

Characterizing the effects of the protein environment on the reduction potentials of metalloproteins

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

The biochemical effect of Ser166 phosphorylation on Euplotes octocarinatus centrin

Elucidating the mechanism of ferrocytochrome c heme disruption by peroxidized cardiolipin

Titanium mineralization in ferritin: a room temperature nonphotochemical preparation and biophysical characterization

Note from the SBIC President

JBIC Journal of Biological Inorganic Chemistry : Volume 17

JBIC Journal of Biological Inorganic Chemistry : Volume 16

JBIC Journal of Biological Inorganic Chemistry : Volume 15

JBIC Journal of Biological Inorganic Chemistry : Volume 14

JBIC Journal of Biological Inorganic Chemistry : Volume 13

JBIC Journal of Biological Inorganic Chemistry : Volume 12

JBIC Journal of Biological Inorganic Chemistry : Volume 11

JBIC Journal of Biological Inorganic Chemistry : Volume 10

JBIC Journal of Biological Inorganic Chemistry : Volume 9

JBIC Journal of Biological Inorganic Chemistry : Volume 8

JBIC Journal of Biological Inorganic Chemistry : Volume 7

JBIC Journal of Biological Inorganic Chemistry : Volume 6

JBIC Journal of Biological Inorganic Chemistry : Volume 5

JBIC Journal of Biological Inorganic Chemistry : Volume 4

JBIC Journal of Biological Inorganic Chemistry : Volume 3

JBIC Journal of Biological Inorganic Chemistry : Volume 2

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

Content Provider	Springer Nature Link
Author	Bocahut, Anthony Derrien, Valérie Bernad, Sophie Sebban, Pierre Sacquin Mora, Sophie Guittet, Eric Lescop, Ewen
Copyright Year	2012
Abstract	Neuroglobin (Ngb) is a globin present in the brain and retina of mammals. This hexacoordinated hemoprotein binds small diatomic molecules, albeit with lower affinity compared with other globins. Another distinctive feature of most mammalian Ngb is their ability to form an internal disulfide bridge that increases ligand affinity. As often seen for prosthetic heme b containing proteins, human Ngb exhibits heme heterogeneity with two alternative heme orientations within the heme pocket. To date, no details are available on the impact of heme orientation on the binding properties of human Ngb and its interplay with the cysteine oxidation state. In this work, we used 1H NMR spectroscopy to probe the cyanide binding properties of different Ngb species in solution, including wild-type Ngb and the single (C120S) and triple (C46G/C55S/C120S) mutants. We demonstrate that in the disulfide-containing wild-type protein cyanide ligation is fivefold faster for one of the two heme orientations (the A isomer) compared with the other isomer, which is attributed to the lower stability of the distal His64–iron bond and reduced steric hindrance at the bottom of the cavity for heme sliding in the A conformer. We also attribute the slower cyanide reactivity in the absence of a disulfide bridge to the tighter histidine–iron bond. More generally, enhanced internal mobility in the CD loop bearing the disulfide bridge hinders access of the ligand to heme iron by stabilizing the histidine–iron bond. The functional impact of heme disorder and cysteine oxidation state on the properties of the Ngb ligand is discussed.
Starting Page	111
Ending Page	122
Page Count	12
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	18
Issue Number	1
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2012-11-08
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	NMR Neuroglobin Molecular dynamics Heme orientation Disulfide bridge Biochemistry Microbiology
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

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

Warfarin modulates the nitrite reductase activity of ferrous human serum heme–albumin

PH-dependent redox and CO binding properties of chelated protoheme-l-histidine and protoheme-glycyl-l-histidine complexes

Kinetics of serotonin oxidation by heme–Aβ relevant to Alzheimer’s disease

Nonadiabatic Histidine Dissociation of Hexacoordinate Heme in Neuroglobin Protein

Modulating carbon monoxide binding affinity and kinetics in myoglobin: the roles of the distal histidine and the heme pocket docking site

Distal mutation modulates the heme sliding in mouse neuroglobin investigated by molecular dynamics simulation

$^{1}$H, $^{15}$N and $^{13}$C Backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

Similar Documents

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin

Warfarin modulates the nitrite reductase activity of ferrous human serum heme–albumin

PH-dependent redox and CO binding properties of chelated protoheme-l-histidine and protoheme-glycyl-l-histidine complexes

Kinetics of serotonin oxidation by heme–Aβ relevant to Alzheimer’s disease

Nonadiabatic Histidine Dissociation of Hexacoordinate Heme in Neuroglobin Protein

Modulating carbon monoxide binding affinity and kinetics in myoglobin: the roles of the distal histidine and the heme pocket docking site

Distal mutation modulates the heme sliding in mouse neuroglobin investigated by molecular dynamics simulation

$^{1}$H, $^{15}$N and $^{13}$C Backbone resonance assignments of murine met-neuroglobin, free and in complex with cyanide

Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin