نتایج جستجو برای: alkyl hydroperoxide reductase

تعداد نتایج: 60341  

2010
T Mohammadian M Doosti M Paknejad F Siavoshi S Massarrat

BACKGROUND Alkyl hydroperoxide reductase (AhpC) of Helicobacter pylori is considered as a diagnostic antigen. Therefore, this antigen can be used to detect H. pylori infection by stool immunoassays such as ELISA. The aim of this study was to simplify the AhpC protein purification procedures. METHODS For whole cell protein extraction, the bacterial cells were ruptured by octly-β-D glucopyranos...

2014
Euna Oh Byeonghwa Jeon

Biofilm formation of Campylobacter jejuni, a major cause of human gastroenteritis, contributes to the survival of this pathogenic bacterium in different environmental niches; however, molecular mechanisms for its biofilm formation have not been fully understood yet. In this study, the role of oxidative stress resistance in biofilm formation was investigated using mutants defective in catalase (...

Journal: :Chemical communications 2014
Ari Zeida Anibal M Reyes Mariano C G Lebrero Rafael Radi Madia Trujillo Darío A Estrin

Peroxiredoxins (Prxs) catalyze the reduction of peroxides, a process of key relevance in a variety of cellular processes. The first step in the catalytic cycle of all Prxs is the oxidation of a cysteine residue to sulfenic acid, which occurs 10(3)-10(7) times faster than in free cysteine. We present an experimental kinetics and hybrid QM/MM investigation to explore the reaction of Prxs with H2O...

2015
Toshiaki Arai Shinya Kimata Daichi Mochizuki Keita Hara Tamotsu Zako Masafumi Odaka Masafumi Yohda Fumio Arisaka Shuji Kanamaru Takashi Matsumoto Shunsuke Yajima Junichi Sato Shinji Kawasaki Youichi Niimura

The NADH oxidase-peroxiredoxin (Prx) system of Amphibacillus xylanus reduces hydroperoxides with the highest turnover rate among the known hydroperoxide-scavenging enzymes. The high electron transfer rate suggests that there exists close interaction between NADH oxidase and Prx. Variant enzyme experiments indicated that the electrons from β-NADH passed through the secondary disulfide, Cys128-Cy...

Journal: :Free radical biology & medicine 2000
L B Poole M Higuchi M Shimada M L Calzi Y Kamio

Nox-1 from Streptococcus mutans, the bacteria which cause dental caries, was previously identified as an H2O2-forming reduced nicotinamide adenine dinucleotide (NADH) oxidase. Nox-1 is homologous with the flavoprotein component, AhpF, of Salmonella typhimurium alkyl hydroperoxide reductase. A partial open reading frame upstream of nox1, homologous with the other (peroxidase) component, ahpC, fr...

Journal: :Journal of bacteriology 2001
L C Seaver J A Imlay

Hydrogen peroxide is generated during aerobic metabolism and is capable of damaging critical biomolecules. However, mutants of Escherichia coli that are devoid of catalase typically exhibit no adverse phenotypes during growth in aerobic media. We discovered that catalase mutants retain the ability to rapidly scavenge H(2)O(2) whether it is formed internally or provided exogenously. Analysis of ...

2014
Ha-Na Lee Na-On Lee Seung J. Han In-Jeong Ko Jeong-Il Oh

The ahpC (MSMEG_4891) gene encodes alkyl hydroperoxide reductase C in Mycobacterium smegmatis mc2155 and its expression is induced under oxidative stress conditions. Two well-defined inverted repeat sequences (IR1 and IR2) were identified in the upstream region of ahpC. Using a crp (cAMP receptor protein: MSMEG_6189) mutant and in vitro DNA-binding assay, it was demonstrated that the IR1 sequen...

Journal: :Biochemistry 2001
C M Reynolds L B Poole

AhpF, the flavoprotein reductase component of the Salmonella typhimurium alkyl hydroperoxide reductase system, catalyzes the reduction of an intersubunit disulfide bond in the peroxidatic active site of the system's other component, AhpC, a member of the peroxiredoxin family. Previous studies have shown that AhpF can be dissected into two functional units, a thioredoxin reductase-like C-terminu...

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