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Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 6
2017 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 56, no 23, 6622-6626 p.Article in journal (Refereed) Published
Abstract [en]

Heme-copper oxidase (HCO) is a class of respiratory enzymes that use a heme-copper center to catalyze O-2 reduction to H2O. While heme reduction potential (E degrees') of different HCO types has been found to vary >500 mV, its impact on HCO activity remains poorly understood. Here, we use a set of myoglobin-based functional HCO models to investigate the mechanism by which heme E degrees' modulates oxidase activity. Rapid stopped-flow kinetic measurements show that increasing heme E degrees' by ca. 210 mV results in increases in electron transfer (ET) rates by 30-fold, rate of O-2 binding by 12-fold, O-2 dissociation by 35-fold, while decreasing O-2 affinity by 3-fold. Theoretical calculations reveal that E degrees' modulation has significant implications on electronic charge of both heme iron and O-2, resulting in increased O-2 dissociation and reduced O-2 affinity at high E degrees' values. Overall, this work suggests that fine-tuning E degrees' in HCOs and other heme enzymes can modulate their substrate affinity, ET rate and enzymatic activity.

Place, publisher, year, edition, pages
2017. Vol. 56, no 23, 6622-6626 p.
Keyword [en]
electron transfer, heme proteins, oxidoreductases, oxygen activation, redox chemistry
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-144701DOI: 10.1002/anie.201701916ISI: 000401791900048PubMedID: 28470988OAI: oai:DiVA.org:su-144701DiVA: diva2:1128052
Available from: 2017-07-21 Created: 2017-07-21 Last updated: 2017-07-21Bibliographically approved

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Kahle, MaximilianÄdelroth, Pia
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