Publication:
Use of a molybdenum(VI) complex as artificial protease in protein photocleavage

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Issued Date

2013

Resource Type

Article

File Type

application/pdf

ISSN

10111344

DOI

10.1016/jjphotobiol.2013.07.004

Other identifier(s)

2-s2.0-84885148422

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Journal of Photochemistry and Photobiology B: Biology. Vol 126, No. (2013), p.55-59

Suggested Citation

Jityuti B., Liwporncharoenvong T., Buranaprapuk A. Use of a molybdenum(VI) complex as artificial protease in protein photocleavage. Journal of Photochemistry and Photobiology B: Biology. Vol 126, No. (2013), p.55-59. doi:10.1016/jjphotobiol.2013.07.004 Retrieved from: https://hdl.handle.net/20.500.14740/6780

Title

Use of a molybdenum(VI) complex as artificial protease in protein photocleavage

Author(s)

Jityuti B.
 Liwporncharoenvong T.
 Buranaprapuk A.

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.

Subject(s)

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

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URI

https://hdl.handle.net/20.500.14740/6780

Collections

Scopus: Year 1983-2021

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