Using Tryptophan Mutants To Probe the Structural andFunctional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis
Using Tryptophan Mutants To Probe the Structural andFunctional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis
NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase [Biochemistry]
NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase
Sakamoto, K., Kamiya, M., Imai, M., Shinzawa-Itoh, K., Uchida, T., Kawano, K., Yoshikawa, S., Ishimori, K....
Date: 2011-07-26
The final interprotein electron transfer (ET) in the mammalian respiratory chain, from cytochrome c (Cyt c) to cytochrome c oxidase (CcO) is investigated by 1H-15N heteronuclear single quantum coherence spectral analysis. The chemical shift perturbation in isotope-labeled Cyt c induced by addition of unlabeled CcO indicates that the hydrophobic heme periphery and...
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[NMR paper] NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
Related Articles NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
J Biomol NMR. 2005 Jul;32(3):258
Authors: Zhang X, Yu C, Xia B, Jin C
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[NMR paper] Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Related Articles Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Biochem Biophys Res Commun. 2005 Sep 23;335(2):361-6
Authors: Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC, Wilce JA
Termination of DNA replication in Bacillus subtilis involves the polar arrest of replication forks by a specific complex formed between the dimeric 29 kDa replication terminator...
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[NMR paper] Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Related Articles Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Biochemistry. 2005 Aug 2;44(30):10153-63
Authors: Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C
Bacillus subtilis CwlC is a cell wall lytic N-acetylmuramoyl-l-alanine amidase that plays an...
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[NMR paper] Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fr
Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Related Articles Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
Biochemistry. 2003 May 27;42(20):6005-12
Authors: Wienk H, Maneg O, Lücke C, Pristovsek P, Löhr F, Ludwig B, Rüterjans H
The functional interactions between the various components of the respiratory chain are relatively short-lived, thus allowing high turnover numbers...
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11-24-2010 09:01 PM
[NMR paper] Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a no
Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a novel 1H NMR spectrum of a 'Tri-Cu(II)' center in protein.
Related Articles Cobalt(II) and copper(II) binding of Bacillus cereus trinuclear phospholipase C: a novel 1H NMR spectrum of a 'Tri-Cu(II)' center in protein.
J Inorg Biochem. 2001 Dec 1;87(3):149-56
Authors: Epperson JD, Ming LJ
The phosphatidylcholine-preferring phospholipase C from Bacillus cereus (PC-PLC(Bc)) is a tri-Zn enzyme with two 'tight binding' and one 'loose binding' sites. The Zn2+ ions can...
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Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Related Articles Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Biochemistry. 2010 Sep 15;
Authors: Chang YC, Franch WR, Oas TG
Protein folding intermediates are often imperative to overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder the biochemical and biophysical characterization. Previous studies have demonstrated that Bacillus...
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[NMR paper] Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-di
Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.
Protein Sci. 1992 Oct;1(10):1363-76
Authors: Wittekind...