Design and preparation of artificial heme-copper enzymes.

Hirbod Heidari, Duong Phan, Danielle Lawson, Yi Lu

Abstract read

In one paragraph

Article in Methods in enzymology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Hirbod HeidariDepartment of Chemistry, The University of Texas at Austin, Austin, TX, United States.

Duong PhanDepartment of Chemistry, The University of Texas at Austin, Austin, TX, United States.

Danielle LawsonDepartment of Chemistry, The University of Texas at Austin, Austin, TX, United States.

Yi LuDepartment of Chemistry, The University of Texas at Austin, Austin, TX, United States. Electronic address: yi.lu@utexas.edu.

Funding

Design and Selection of Novel Metalloenzymes for Biocatalysis, Bioimaging, and Genetic EngineeringR35GM141931 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Yi Lu · 2021 to 2026

$3.5M

NIGMS NIH HHS R35 GM141931

6 · The paper itself

Abstract

Natural and artificial metalloproteins play a critical role in biochemistry, with the first X-ray crystal structures ever solved belonging to heme proteins Due to their ability to carry out a diverse array of challenging reactions at ambient temperature, effective metalloenzyme design and isolation strategies are highly desirable. Control of active site geometry is often the key requirement for catalysis and its mutagenesis helps probe a wide variety of biological and abiological reactions. In the case of small-molecule activation, introduction of new metal-binding sites to non-native heme scaffolds can unlock new chemistry. In this chapter, we will provide methods used in our lab for the design and experimental preparation of artificial metalloenzymes containing a heme-copper center to mimic and understand heme-copper oxidases. The methods can be applied to design other heterobinuclear centers containing heme, such as the heme-nonheme iron center in nitric oxidase reductases.

Indexed as

CopperHemeMetalloproteinsOxidoreductasesProtein EngineeringCatalytic DomainCrystallography, X-RayModels, MolecularCoppercopper oxidaseHemeMetalloproteinsOxidoreductasesArtificial metalloenzymesComputational designProtein designprotein purification

Identifiers

PMID41047215

DOI10.1016/bs.mie.2025.08.004

PMCPMC12966992

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.