Author

Zhiyao Zhang

Western Michigan UniversityORCID 0000-0002-6974-373XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Organism:bacteria (other)· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:experimental assay· 1 Research Focus:protein design· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

Frederick W. StulliD· 2 shared Andrew J. Gaunt· 1 shared Kaitrin Freeland· 1 shared Parth R BandivadekariD· 1 shared Surl-Hee AhniD· 1 shared Todd J. BarkmaniD· 1 shared

Activity by Year

2025-2025 · peak 2/yr

Co-Author Collaboration Network

6 top collaborators · 11 mutual co-author links

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2 shared papersBiochemistry

Frederick W. StullORCID

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2 papers

Recent·Most cited

BiochemistryJournal of Biological ChemistryPeer-reviewedJun 11, 2025

Ancestral evolution of oxidase activity in a class of (S)-nicotine and (S)-6-hydroxynicotine degrading flavoenzymes

Zhiyao Zhang, Parth R Bandivadekar, Andrew J. Gaunt…·Frederick W. Stull

This study traces the evolutionary emergence of oxidase activity in nicotine-degrading flavoenzymes by identifying key amino acid changes and their structural impacts.

3 citations

statistical modelchromatin & epigenetic regulation

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BiochemistryArchives of Biochemistry and BiophysicsPeer-reviewedMay 31, 2025

Role of glutamate 292 and lysine 331 in catalysis for the flavoenzyme (S)-6-hydroxynicotine oxidase from Shinella sp. HZN7

Zhiyao Zhang, Kaitrin Freeland, Frederick W. Stull

This study identifies Glu292 and Lys331 as critical residues in NctB's catalytic mechanism, showing that Glu292 optimizes Lys331's role in dioxygen activation despite lacking the conserved lysine found in other FAO enzymes.

2 citations

bacteria (other)proteomics

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