NMR paper 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from

		BioNMR > Educational resources > Journal club
[NMR paper] 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-21-2010, 11:53 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,700

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from

1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.

Related Articles 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.

Eur J Biochem. 1993 Feb 15;212(1):69-78

Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M

1H one-dimensional and two-dimensional NMR spectra have been recorded for the oxidized and reduced forms of the high-potential iron-sulfur protein (HiPIP) from Rhodopseudomonas globiformis which has the highest known reduction potential. The spectrum of the oxidized protein is similar to that of Chromatium vinosum and Rhodocyclus gelatinosus HiPIP but different from that of the HiPIP II from Ectothiorhodospira halophila. Surprisingly, site-specific assignment has shown that in the oxidized protein the distribution of oxidation numbers within the cluster is very similar to that found for E. halophila HiPIP II and different from that of the other two proteins. The spectrum of the reduced species is very similar to that of all other HiPIPs known to date, indicating very similar electronic and geometric structures for the reduced forms. These findings are discussed in terms of cluster structure in HiPIPs and of redox potentials.

PMID: 8444166 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site. Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site. J Mol Biol. 2004 Nov 19;344(2):567-83 Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins. Related Articles 13C-, 15N- and 31P-NMR studies of oxidized and reduced low molecular mass thioredoxin reductase and some mutant proteins. Eur J Biochem. 2004 Apr;271(8):1437-52 Authors: Eisenreich W, Kemter K, Bacher A, Mulrooney SB, Williams CH, Müller F Thioredoxin reductase (TrxR) from Escherichia coli, the mutant proteins E159Y and C138S, and the mutant protein C138S treated with phenylmercuric acetate were...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Identification of slow motions in the reduced recombinant high-potential iron sulfur Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements. Related Articles Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements. J Biomol NMR. 1998 Aug;12(2):307-18 Authors: Banci L, Felli IC, Koulougliotis D Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues. Related Articles Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues. Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80 Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhod 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans. Eur J Biochem. 1996 Mar 1;236(2):405-11 Authors: Ciurli S, Cremonini MA, Kofod P, Luchinat C Oxidized and reduced forms of high-potential iron-sulfur protein (HiPIP) from the...	nmrlearner	Journal club	0	08-22-2010 02:27 PM
[NMR paper] Three-dimensional solution structure of the oxidized high potential iron-sulfur prote Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Related Articles Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Biochemistry. 1995 Aug 8;34(31):9851-8 Authors: Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P The NMR solution structure of...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] The three-dimensional solution structure of the reduced high-potential iron-sulfur pr The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Related Articles The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Biochemistry. 1995 Jan 10;34(1):206-19 Authors: Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature has been extended up to 85% of the total protein protons. Ninety...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nucle 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements. Related Articles 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements. Biochemistry. 1990 Jun 12;29(23):5633-7 Authors: Cowan JA, Sola M 1H nuclear Overhauser effect experiments on the isotropically shifted signals of oxidized Chromatium vinosum HiPIP have been used to identify the four beta-CH2 geminal couples of the cysteine ligands. A partial assignment to...	nmrlearner	Journal club	0	08-21-2010 10:48 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off