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Insights Into How H...
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Bhagi-Damodaran, Ambika
(författare)
Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase
- Artikel/kapitelEngelska2017
Förlag, utgivningsår, omfång ...
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2017-05-04
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Wiley,2017
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printrdacarrier
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LIBRIS-ID:oai:DiVA.org:su-144701
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https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-144701URI
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https://doi.org/10.1002/anie.201701916DOI
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Språk:engelska
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Sammanfattning på:engelska
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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.
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Kahle, MaximilianStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)mkahl
(författare)
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Shi, Yelu
(författare)
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Zhang, Yong
(författare)
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Ädelroth, PiaStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)adelr
(författare)
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Lu, Yi
(författare)
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Stockholms universitetInstitutionen för biokemi och biofysik
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Angewandte Chemie International Edition: Wiley56:23, s. 6622-66261433-78511521-3773
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