R P Swenson
Overview
Explore the profile of R P Swenson including associated specialties, affiliations and a list of published articles.
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Articles
45
Citations
446
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Recent Articles
1.
Rotello V, Swenson R
Antioxid Redox Signal
. 2002 Jan;
3(5):721-2.
PMID: 11761321
No abstract available.
2.
Kasim M, Swenson R
Biochemistry
. 2001 Nov;
40(45):13548-55.
PMID: 11695902
The four-residue reverse turn -Met56-Gly-Asp-Glu59- in the Clostridium beijerinckii flavodoxin provides the majority of the critical interactions with the isoalloxazine ring of the flavin mononucleotide (FMN) cofactor that contribute to...
3.
Bradley L, Swenson R
Biochemistry
. 2001 Jul;
40(30):8686-95.
PMID: 11467928
The role of the hydrogen bonding interaction with the N(3)H of the flavin cofactor in the modulation of the redox properties of flavoproteins has not been extensively investigated. In the...
4.
Chang F, Bradley L, Swenson R
Biochim Biophys Acta
. 2001 Mar;
1504(2-3):319-28.
PMID: 11245795
The oxidation-reduction potentials for the riboflavin complex of the Desulfovibrio vulgaris flavodoxin are substantially different from those of the flavin mononucleotide (FMN) containing native protein, with the midpoint potential for...
5.
Kasim M, Swenson R
Biochemistry
. 2000 Dec;
39(50):15322-32.
PMID: 11112518
A surface loop in the flavodoxin from Clostridium beijerinckii comprised of residues -Met(56)-Gly-Asp-Glu(59)- forms a four-residue reverse turn which undergoes a conversion from a mix of cis/trans peptide configurations that...
6.
Bradley L, Swenson R
Biochemistry
. 1999 Sep;
38(38):12377-86.
PMID: 10493805
The midpoint potentials for both redox couples of the noncovalently bound flavin mononucleotide (FMN) cofactor in the flavodoxin are known to be pH dependent. While the pH dependency for the...
7.
Chang F, Swenson R
Biochemistry
. 1999 Jun;
38(22):7168-76.
PMID: 10353827
In the Clostridium beijerinckii flavodoxin, the reduction of the flavin mononucleotide (FMN) cofactor is accompanied by a local conformation change in which the Gly57-Asp58 peptide bond "flips" from primarily the...
8.
Druhan L, Swenson R
Biochemistry
. 1998 Jul;
37(27):9668-78.
PMID: 9657679
Flavodoxins are small electron transferases that participate in low-potential electron transfer pathways. The flavodoxin protein is able to separate the two redox couples of the noncovalently bound flavin mononucleotide (FMN)...
9.
Feng Y, Swenson R
Biochemistry
. 1997 Nov;
36(44):13617-28.
PMID: 9354631
A hypothetical model for electron transfer complex between cytochrome c3 and the flavodoxin from the sulfate-reducing bacteria Desulfovibrio vulgaris has been proposed, based on electrostatic potential field calculations and NMR...
10.
Chang F, Swenson R
Biochemistry
. 1997 Jul;
36(29):9013-21.
PMID: 9220989
Flavodoxin from Desulfovibrio vulgaris is a low molecular weight (15 000 Da) acidic flavoprotein that contains a single flavin mononucleotide (FMN) cofactor. A distinguishing feature of the flavodoxin family is...