A Caltech Library Service

Reactive intermediates in multicopper oxidase catalysis

Shin, Jieun and Winkler, Jay Richmond and Gray, Harry B. (2019) Reactive intermediates in multicopper oxidase catalysis. In: 258th ACS National Meeting & Exposition, 25-29 August 2019, San Diego, CA.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


In the past few decades, there has been growing interest in using metalloenzymes for improved biomass degrdn. and utilization. Multicopper oxidases (MCOs) are lignin degrading enzymes with four copper sites (Figure 1): a type 1 Cu center (Cu_(T1)) is involved in substrate oxidn. and electron transfer to a trinuclear Cu center (TNC) where O_2 is reduced to H_2O. The MCO of interest in this study is from the HB27 strain of the thermophilic bacterium Thermus thermophilus; it is stable and active even above 90°C. The enzyme is active for lignin oxidn., although the potential of Cu_(T1) (E°(Cu2+/+) = 0.53 V vs. NHE, pH 4.5) is lower than that expected for one-electron oxidn. of methoxy phenols. It is important, therefore, to elucidate the mechanistic details of substrate oxidn. by characterizing electron-transfer pathways and trapping reactive intermediates crit. for enzyme catalysis and function. Detn. of crit. residues for enzyme catalysis as well as gaining a deeper understanding of the redox chem. involved in the catalytic pathways of MCOs will facilitate the development of more energy-efficient and environmentally friendly biocatalysts.

Item Type:Conference or Workshop Item (Paper)
Related URLs:
URLURL TypeDescription Website
Winkler, Jay Richmond0000-0002-4453-9716
Gray, Harry B.0000-0002-7937-7876
Additional Information:© 2019 American Chemical Society.
Record Number:CaltechAUTHORS:20190812-090439146
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:97751
Deposited By: Tony Diaz
Deposited On:12 Aug 2019 17:31
Last Modified:22 Nov 2019 09:58

Repository Staff Only: item control page