NDLI: Carbon monoxide binding properties of domain-swapped dimeric myoglobin

Content Provider	Springer Nature Link
Author	Nagao, Satoshi Ishikawa, Haruto Yamada, Takuya Mizutani, Yasuhisa Hirota, Shun
Copyright Year	2015
Abstract	Myoglobin (Mb) is a monomeric oxygen storage hemoprotein, and has been shown to form a domain-swapped dimer. In this study, monomeric and dimeric carbon monoxide (CO)-bound Mb (MbCO) exhibited similar absorption spectra. The CO stretching frequencies of MbCO were observed at 1,932 and 1,944 cm−1 for both monomeric and dimeric MbCO. The resonance Raman (RR) bands for the stretching between the heme iron and axial ligands were observed at the same frequencies for the monomer and dimer of deoxygenated Mb (deoxyMb) and MbCO, respectively (ν Fe–His, 220 cm−1; ν Fe–C, 507 cm−1), showing that the Fe–His bond strength of deoxyMb and the Fe–CO bond strength of MbCO did not change by the dimerization. Time-resolved RR measurements showed that the dynamics of the structural changes at the heme active site after CO photo-dissociation of MbCO was similar between monomeric and dimeric Mb [monomer, (5.2 ± 1.8) × 106 s−1; dimer, (6.2 ± 1.1) × 106 s−1 at room temperature]. These results show that the heme coordination structure, the protein environment around the bound CO, and the protein relaxation character are similar between monomeric and dimeric MbCO. Although the active site structure was similar between the monomer and dimer, the CO binding rate constant of dimeric Mb [(1.01 ± 0.03) × 106 M−1 s−1 at 20 °C] was about twice larger than that of the monomer [(0.52 ± 0.02) × 106 M−1 s−1 at 20 °C], presumably due to the expansion of the channel between the Xe3 cavity and the solvent by the dimerization.
Starting Page	523
Ending Page	530
Page Count	8
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	20
Issue Number	3
e-ISSN	14321327
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2015-01-13
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Myoglobin Domain swapping Ligand binding Active site structure 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

Carbon monoxide binding properties of domain-swapped dimeric myoglobin.

IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase

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

Formation and carbon monoxide-dependent dissociation ofAllochromatium vinosumcytochromec′ oligomers using domain-swapped dimers

Interaction of dimeric horse cytochrome c with cyanide ion

Interaction of the active site of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough with carbon monoxide and oxygen inhibitors

The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy

Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin

19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin

Carbon monoxide binding properties of domain-swapped dimeric myoglobin

Similar Documents

Carbon monoxide binding properties of domain-swapped dimeric myoglobin.

IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase

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

Formation and carbon monoxide-dependent dissociation ofAllochromatium vinosumcytochromec′ oligomers using domain-swapped dimers

Interaction of dimeric horse cytochrome c with cyanide ion

Interaction of the active site of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough with carbon monoxide and oxygen inhibitors

The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy

Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin

19F NMR study of protein-induced rhombic perturbations on the electronic structure of the active site of myoglobin

Carbon monoxide binding properties of domain-swapped dimeric myoglobin