NMR paper Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing su

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[NMR paper] Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing su

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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

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NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

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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

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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08-22-2010, 03:50 AM

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Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing su

Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion-binding studies.

Related Articles Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion-binding studies.

Eur J Biochem. 1995 Oct 1;233(1):335-9

Authors: Battistuzzi G, Borsari M, Dallari D, Ferretti S, Sola M

The effects of increasing concentrations of Cl-, ClO4-, and HCO3- on the redox potential of Rhodopseudomonas palustris cytochrome c2 indicate that the two polyatomic anions bind specifically to the protein at one site, while chloride simply exerts an ionic atmosphere effect. The change in E degree upon specific anion binding allows us to probe for the influence of surface charges on the redox potential of cytochromes c. The decrease in redox potential at null ionic strength (delta E degree I = 0) due to anion neutralization of one positive surface charge was found to be 23 mV with perchlorate and 33 mV with bicarbonate. These values compare reasonably well with previous theoretical predictions and estimates of the effect of charge alteration on the E degree values in cytochromes c chemically modified or mutated at surface lysines. These delta E degree values, determined on the unmodified protein, are unprecedented for c-type cytochromes. The anion-induced chemical shift changes of the hyperfine-shifted heme 1H-NMR resonances of the oxidized protein yield lower limit values of 53 M-1 and 18 M-1 for the affinity constant for specific HCO3- and ClO4- binding, respectively.

PMID: 7588763 [PubMed - indexed for MEDLINE]

Source: PubMed

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