NDLI: Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes

Please wait, while we are loading the content...

Crystal and molecular structure of 2-hydroxy-1-naphthaldehyde isonicotinoyl hydrazone (NIH) and its iron(III) complex: an iron chelator with anti-tumour activity

The effect of iron to manganese substitution on microperoxidase 8 catalysed peroxidase and cytochrome P450 type of catalysis

On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry

EPR properties of mixed-valent μ-oxo and μ-hydroxo dinuclear iron complexes produced by radiolytic reduction at 77 K

Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin

The [2Fe-2S] protein I (Shetna protein I) from Azotobacter vinelandii is homologous to the [2Fe-2S] ferredoxin from Clostridium pasteurianum

Trans-pyridine tetraammine complexes of RuII and RuIII with N7-coordninated purine nucleosides

Effects of trans-pyridine ligands on the interactions of RuII and RuIII ammine complexes N7-coordinated to purine nucleosides and DNA

Synthesis and physicochemical characterization of a novel precursor for covalently bound macromolecular MRI contrast agents

The metal function in the reactions of bovine serum amine oxidase with substrates and hydrazine inhibitors

Vanadate inhibition of protein tyrosine phosphatases in Jurkat cells: modulation by redox state

Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes

JBIC Journal of Biological Inorganic Chemistry : Volume 4, Issue 2, May 1999

JBIC Journal of Biological Inorganic Chemistry : Volume 4, Issue 1, February 1999

JBIC Journal of Biological Inorganic Chemistry : Volume 3

JBIC Journal of Biological Inorganic Chemistry : Volume 2

Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes

Content Provider	Springer Nature Link
Author	Cunha, Carlos A. Romão, Maria J. Sadeghi, Sheila J. Valetti, F. Gilardi, G. Soares, Cláudio M.
Copyright Year	1999
Abstract	Theoretical studies of protein-protein association and electron transfer were performed on the binary systems formed by Desulfovibrio vulgaris Hildenborough (D. v. H.) flavodoxin and D. v. H. cytochrome c 553 and by flavodoxin and horse heart cytochrome c. Initial structures for the complexes were obtained by rigid-body docking and were refined by MD to allow for molecular flexibility. The structures thus obtained were analysed in terms of their relative stability through the calculation of excess energies. Electrostatic, van der Waals and solvation energy terms showed all to have significant contributions to the stability of complexes. In the best association solutions found for both cytochromes, these bind to different zones of flavodoxin. The binding site of flavodoxin observed for cytochrome c is in accordance with earlier works [27]. The various association modes found were characterised in terms of electron transfer using the Pathways model. For complexes between flavodoxin and horse heart cytochrome c, some correlation was observed between electron tunnelling coupling factors and conformation energy; the best conformation found for electron transfer corresponded also to the best one in terms of energy. For complexes between flavodoxin and cytochrome c 553 this was not the case and a lower correlation was observed between electron tunnelling coupling factors and excess energies. These results are in accordance with the differences in the experimental dependence of electron transfer rates with ionic strength observed between these two cases.
Starting Page	360
Ending Page	374
Page Count	15
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	4
Issue Number	3
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	1999-07-02
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
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

Electrostatic interactions during electron transfer reactions between c-type cytochromes and flavodoxin.

A systematic investigation of multiheme c-type cytochromes in prokaryotes

The electron transfer complex between nitrous oxide reductase and its electron donors

Ionic strength dependence of the non-physiological electron transfer between flavodoxin and cytochrome c 553 from D. vulgaris

A structural model for the adduct between cytochrome c and cytochrome c oxidase

Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp

Protein-protein interactions in the systems of cytochromes P450 3A4 and 3A5

Docking and electron transfer studies between rubredoxin and rubredoxin:oxygen oxidoreductase

A method and program for mass quantum chemical calculations of protein—ligand docking complexes

Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes

Similar Documents

Electrostatic interactions during electron transfer reactions between c-type cytochromes and flavodoxin.

A systematic investigation of multiheme c-type cytochromes in prokaryotes

The electron transfer complex between nitrous oxide reductase and its electron donors

Ionic strength dependence of the non-physiological electron transfer between flavodoxin and cytochrome c 553 from D. vulgaris

A structural model for the adduct between cytochrome c and cytochrome c oxidase

Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp

Protein-protein interactions in the systems of cytochromes P450 3A4 and 3A5

Docking and electron transfer studies between rubredoxin and rubredoxin:oxygen oxidoreductase

A method and program for mass quantum chemical calculations of protein—ligand docking complexes

Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes