Related ArticlesThe dynamics of lysine as a heme axial ligand: NMR analysis of the Chlamydomonas reinhardtii hemoglobin THB1.
Biochemistry. 2016 Dec 29;:
Authors: Preimesberger MR, Majumdar A, Lecomte JT
Abstract
Nitrate metabolism in Chlamydomonas reinhardtii involves THB1, a monomeric hemoglobin thought to function as a nitric oxide dioxygenase (NOD). NOD activity requires dioxygen and nitric oxide binding followed by a one-electron oxidation of the heme iron and nitrate release. Unlike pentacoordinate flavohemoglobins, which are efficient NODs, THB1 uses two iron axial ligands: the conserved proximal histidine and a distal lysine (Lys53). As a ligand in both the oxidized (ferric) and reduced (ferrous) states, Lys53 is expected to lower the reorganization energy associated with electron transfer and therefore facilitate reduction of the ferric enzyme. In ferrous THB1, however, Lys53 must be displaced for substrate binding. To characterize Lys53 dynamics, THB1 was studied at various pH, temperatures, and pressures by NMR spectroscopy. Structural information indicates that the protein fold and Lys53 environment are independent of oxidation state. High-pressure NMR experiments provided evidence that displacement of Lys53 occurs through fast equilibrium (~ 3-4 x 10(3) s(-1) at 1 bar, 298 K) with a low-population intermediate in which Lys53 is neutral and decoordinated. Once decoordinated, Lys53 is able to orient toward solvent and become protonated. The global lysine decoordination/reorientation/protonation processes measured by (15)Nz-exchange spectroscopy are slow on the chemical shift time scale (10(1)-10(2) s(-1) at pH ~ 6.5, 298 K) in both iron redox states. Thus, reorientation/protonation steps in ferrous THB1 appear to present a significant barrier for dioxygen binding, and consequently, NOD turnover. The results illustrate the role of distal ligand dynamics in regulating the kinetics of multi-step heme redox reactions.
PMID: 28032976 [PubMed - as supplied by publisher]
[NMR paper] (1)H, (13)C and (15)N NMR assignments of Mg (2+) bound form of UV inducible transcript protein (UVI31+) from Chlamydomonas reinhardtii.
(1)H, (13)C and (15)N NMR assignments of Mg (2+) bound form of UV inducible transcript protein (UVI31+) from Chlamydomonas reinhardtii.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles (1)H, (13)C and (15)N NMR assignments of Mg (2+) bound form of UV inducible transcript protein (UVI31+) from Chlamydomonas reinhardtii.
Biomol NMR Assign. 2014 Mar 18;
Authors: Singh H, Verma D, Rao BJ, Chary KV
Abstract
Almost complete sequence specific...
nmrlearner
Journal club
0
03-19-2014 10:43 PM
[NMR paper] Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts.
Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts.
Related Articles Artificial heme-proteins: determination of axial ligand orientations through paramagnetic NMR shifts.
Chem Commun (Camb). 2014 Mar 3;
Authors: Vicari C, Saraiva IH, Maglio O, Nastri F, Pavone V, Louro RO, Lombardi A
Abstract
An empirical equation, describing the relationship between the porphyrin methyl hyperfine shifts and the position of the axial ligand(s), has been applied to an artificial heme-protein in order to...
nmrlearner
Journal club
0
03-04-2014 06:37 PM
[NMR paper] The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures.
The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures.
The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures.
Proteins. 2013 Sep 2;
Authors: Wenke BB, Lecomte JT, Héroux A, Schlessman JL
Abstract
The X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 Å resolution) and cyanide-bound (2.25 Å resolution)...
nmrlearner
Journal club
0
09-04-2013 12:28 PM
[NMR paper] (1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii.
(1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii.
(1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii.
Biomol NMR Assign. 2013 Aug 27;
Authors: Singh H, Rao BJ, Chary KV
Abstract
Almost complete sequence specific (1)H, (13)C and (15)N resonance assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii are reported, as a prelude to its structural and functional...
nmrlearner
Journal club
0
08-28-2013 11:43 AM
[NMR paper] Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study.
Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study.
Related Articles Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high-pressure NMR study.
Biochim Biophys Acta. 2013 Apr 22;
Authors: Dellarole M, Roumestand C, Royer C, Lecomte JT
Abstract
The 2/2 hemoglobin of the cyanobacterium Synechococcus sp. PCC 7002, GlbN, coordinates the heme iron with two histidines and exists either with a b heme or with a covalently attached heme. The binding of exogenous ligands...
nmrlearner
Journal club
0
04-27-2013 01:56 PM
[NMR paper] Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
Inorg Chem. 2013 Jan 17;
Authors: Abriata LA, Zaballa ME, Berry RE, Yang F, Zhang H, Walker FA, Vila AJ
Abstract
The electronic structure of heme proteins is exquisitely tuned...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
[NMR paper] Axial ligand modulation of the electronic structures of binuclear copper sites: analy
Axial ligand modulation of the electronic structures of binuclear copper sites: analysis of paramagnetic 1H NMR spectra of Met160Gln Cu(A).
Related Articles Axial ligand modulation of the electronic structures of binuclear copper sites: analysis of paramagnetic 1H NMR spectra of Met160Gln Cu(A).
J Am Chem Soc. 2001 Nov 28;123(47):11678-85
Authors: Fernández CO, Cricco JA, Slutter CE, Richards JH, Gray HB, Vila AJ
Cu(A) is an electron-transfer copper center present in heme-copper oxidases and N2O reductases. The center is a binuclear unit, with...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii
The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
Related Articles The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
Eur J Biochem. 1998 Jul 1;255(1):185-95
Authors: Krimm I, Lemaire S, Ruelland E, Miginiac-Maslow M, Jaquot JP, Hirasawa M, Knaff DB, Lancelin JM
The role of the invariant Trp...
The dynamics of lysine as a heme axial ligand: NMR analysis of the Chlamydomonas reinhardtii hemoglobin THB1.
Linear Mode
