Redox control of protein conformation in flavoproteins

T Senda, M Senda, S Kimura, T Ishida - Antioxidants & Redox …, 2009 - liebertpub.com
Flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are two flavin
prosthetic groups utilized as the redox centers of various proteins. The conformations and …

Complete genome sequence of Acidovorax sp. strain KKS102, a polychlorinated-biphenyl degrader

Y Ohtsubo, F Maruyama, H Mitsui, Y Nagata, M Tsuda - 2012 - Am Soc Microbiol
Complete Genome Sequence of Acidovorax sp. Strain KKS102, a Polychlorinated-Biphenyl
Degrader | Journal of Bacteriology CLOSE This Journal Anywhere Enter words / phrases / DOI …

Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin

M Senda, S Kishigami, S Kimura, M Fukuda… - Journal of molecular …, 2007 - Elsevier
The electron transfer system of the biphenyl dioxygenase BphA, which is derived from
Acidovorax sp.(formally Pseudomonas sp.) strain KKS102, is composed of an FAD …

Anaerobic crystallization of proteins

M Senda, T Senda - Biophysical Reviews, 2018 - Springer
Crystallization has been a bottleneck in the X-ray crystallography of proteins. Although many
techniques have been developed to overcome this obstacle, the impurities caused by …

[图书][B] Structure function analysis of nitrobenzene 1, 2-dioxygenase

KM Mahan - 2014 - search.proquest.com
Structures are available for closely related electron transfer components (ferredoxin and
reductase). Structural data were used to identify residues on the surface of the oxygenase …

[PDF][PDF] Complete Genome Sequence of Acidovorax sp. Strain KKS102, a Polychlorinated-Biphenyl Degrader

NGB under accession number CP003872 - academia.edu
KKS102, a betaproteobacterial Acidovorax sp. strain, was isolated from a mixed culture that
degrades biphenyl/polychlorinated biphenyls (biphenyl/PCB). KKS102 was not able to grow …

Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type ferredoxin

M Senda, S KIMURA, M FUKUDA, T ISHIDA… - Nihon Kessho …, 2008 - jstage.jst.go.jp
Redox-dependent affinity regulation is critical to fast and efficient electron transfer (ET)
between ET proteins. The molecular mechanism of the affinity regulation, however, remains …

電子伝達タンパク質間の酸化還元状態依存的親和性調節機構

千田美紀, 木村成伸, 福田雅夫, 石田哲夫, 千田俊哉 - 化学と生物, 2008 - jstage.jst.go.jp
抄録 電子伝達タンパク質間の酸化還元状態依存的な親和性調節機構は, 長年にわたり多くの研究
者の興味の的であった. 著者らは, 芳香環水酸化ジオキシゲナーゼの電子伝達系を構成する 2 …

反応中間体構造から明らかになった電子伝達タンパク質間の酸化還元依存的な親和性調節機構

千田美紀, 木村成伸, 福田雅夫, 石田哲夫, 千田俊哉 - 日本結晶学会誌, 2008 - jlc.jst.go.jp
Redox-dependent affinity regulation is critical to fast and efficient electron transfer (ET)
between ET proteins. The molecular mechanism of the affinity regulation, however, remains …

[引用][C] 電子伝達タンパク質間の酸化還元状態依存的な親和性調節機構の解明

福田雅夫, 曽田邦嗣, 田中信忠, 論文目次, 第一部