Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/14154
Title: Use of a molybdenum(VI) complex as artificial protease in protein photocleavage
Authors: Jityuti B.
Liwporncharoenvong T.
Buranaprapuk A.
Keywords: alcohol
alpha amino acid
hydroxyl radical
leucine
molybdenum complex
molybdenum peroxo alpha amino acid complex
pepsin A
proteinase
unclassified drug
absorption
amino acid sequence
article
binding site
concentration (parameters)
controlled study
irradiation
metal binding
molecular weight
nonhuman
pH
photochemistry
priority journal
protein cleavage
protein interaction
reaction time
room temperature
sequence analysis
swine
ultraviolet radiation
Sus
Cleavage reactions
Molybdenum complex
Pepsin
Protein-metal interactions
Transition metals
Amino Acid Sequence
Animals
Binding Sites
Biomimetic Materials
Ethanol
Molybdenum
Organometallic Compounds
Pepsin A
Peptide Hydrolases
Photochemical Processes
Proteolysis
Substrate Specificity
Swine
Issue Date: 2013
Abstract: In this study, a molybdenum(VI) peroxo a-amino acid complex, MoO(O 2)2(a-leucine) (H2O), was prepared and used as an artificial protease for site-specific cleavage of porcine pepsin, a model protein. Cleavage of pepsin by MoO(O2)2(a-leucine) (H 2O) was achieved under photochemical conditions at room temperature and pH 7.0. The reaction was activated by irradiation of the MoO(O 2)2(a-leucine) (H2O)-pro-tein mixture by UV light (320 and 340 nm) for up to 30 min. No cleavage was observed in the absence of MoO(O2)2(a-leucine) (H2O) or the light. The photocleavage yield increased with irradiation time. The cleaved fragments were sequencable, and the cleavage site was assigned to Leu(112)-Tyr(113). The cleavage reaction was quenched by ethanol. Therefore, hydroxyl radicals may be involved in the reaction and responsible for the cleavage of the protein. This is the first demonstration of the successful photoc-leavage of proteins by a molybdenum complex. This observation can provide a new approach for the photochemical footprinting of metal binding sites on proteins. © 2013 Elsevier Ltd. All rights reserved.
URI: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84885148422&doi=10.1016%2fjjphotobiol.2013.07.004&partnerID=40&md5=509497653add9510b63542ecd9ac625d
http://ir.swu.ac.th/jspui/handle/123456789/14154
ISSN: 10111344
Appears in Collections:Scopus 1983-2021

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