NDLI: Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme <i>b</i> proteins, the nitrophorins

Content Provider	Royal Society of Chemistry (RSC)
Author	Ogata, Hideaki Lubitz, Wolfgang He, Chunmao
Copyright Year	2016
Abstract	Nitrophorins (NPs) catalyze the nitrite dismutation reaction that is unprecedented in ferriheme proteins. Despite progress in studying the reaction mechanism, fundamental issues regarding the correlation of the structural features with the nitrite dismutase activity of NPs remain elusive. On the other hand, it has been shown that the nitrite complexes of NPs are unique among those of the ferriheme proteins since some of their electron paramagnetic resonance (EPR) spectra show significant highly anisotropic low spin (HALS) signals with large gmax values over 3.2. The origin of HALS signals in ferriheme proteins or models is not well understood, especially in cases where axial ligands other than histidine are present. In this study several mutations were introduced in NP4. The related nitrite coordination and dismutation reaction were investigated. As a result, the EPR spectra of the NP–nitrite complexes were found to be tightly correlated with the extent of heme ruffling and protonation state of the proximal His ligand—dictated by an extended H-bonding network at the heme active site. Furthermore, it is established that the two factors are essential in determining the nitrite dismutase activity of NPs. These results may provide a valuable guide for identifying or designing novel heme proteins with similar activity.
Starting Page	5332
Ending Page	5340
Page Count	9
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	7
Issue Number	8
Journal	Chemical Science
DOI	10.1039/c6sc01019a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	HALS NP Disproportionation Histidine Anisotropy EPR Active site Reaction mechanism Nitrite Electron paramagnetic resonance
Content Type	Text
Resource Type	Article
Subject	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

Assignment of the ferriheme resonances of high- and low-spin forms of the symmetrical hemin-reconstituted nitrophorins 1–4 by 1H and 13C NMR spectroscopy: the dynamics of heme ruffling deformations

Analyzing heme proteins using EPR techniques: the heme-pocket structure of ferric mouse neuroglobin

Three coordinate models for the binuclear Cu_A electron-transfer site

A traffic light enzyme: acetate binding reversibly switches chlorite dismutase from a red- to a green-colored heme protein.

Review: Studies of ferric heme proteins with highly anisotropic/highly axial low spin (S= 1/2) electron paramagnetic resonance signals with bis-Histidine and histidine-methionine axial iron coordination

Unusual flexibility of distal and proximal histidine residues in the haem pocket of Drosophila melanogaster haemoglobin

Mechanism of the reaction of bovine copper–zinc superoxide dismutase. An electron spin resonance study

Computer modeling of nitroxide spin labels on proteins

Beyond structure: Deciphering site-specific dynamics in proteins from double histidine-based EPR measurements.

Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins

Similar Documents

Assignment of the ferriheme resonances of high- and low-spin forms of the symmetrical hemin-reconstituted nitrophorins 1–4 by 1H and 13C NMR spectroscopy: the dynamics of heme ruffling deformations

Analyzing heme proteins using EPR techniques: the heme-pocket structure of ferric mouse neuroglobin

Three coordinate models for the binuclear CuA electron-transfer site

A traffic light enzyme: acetate binding reversibly switches chlorite dismutase from a red- to a green-colored heme protein.

Review: Studies of ferric heme proteins with highly anisotropic/highly axial low spin (S= 1/2) electron paramagnetic resonance signals with bis-Histidine and histidine-methionine axial iron coordination

Unusual flexibility of distal and proximal histidine residues in the haem pocket of Drosophila melanogaster haemoglobin

Mechanism of the reaction of bovine copper–zinc superoxide dismutase. An electron spin resonance study

Computer modeling of nitroxide spin labels on proteins

Beyond structure: Deciphering site-specific dynamics in proteins from double histidine-based EPR measurements.

Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferriheme b proteins, the nitrophorins

Three coordinate models for the binuclear Cu_A electron-transfer site