The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase

Shersher, Elena

doi:10.25148/etd.fidc000241

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Introduction1

Distal Cpo Mutants Activity References N74v N74q1

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References 110 publications

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“…Within the proximal pocket of CPO, there is a hydrogen bonding network form between helix A and the nearby loop, Arg26-Asn37 and Ala27-Asn33, as observed in Figure 2.1. This hydrogen bonding network is previously studied in our research lab and shown to play an important role in maintaining the secondary and tertiary structure of CPO as well as other spectroscopic properties of the enzyme [126]. In CPO, another type of hydrogen bonding network is also found in the proximal region, which is the amide-sulfur hydrogen bonding network.…”

Section: Introductionmentioning

confidence: 79%

“…No sign of chlorination and dismutation activities, increased in epoxidation and peroxidation activities [124] H105A Increased in epoxidation activity, decreased in chlorination and dismutation activity [123] E183H Increased in epoxidation activity, decreased in chlorination and dismutation activities [125] F186A R26A/N33A No sign of chlorination and dismutation activities, increased in epoxidation and peroxidation activities [126] CHAPTER II.…”

Section: Distal Cpo Mutants Activity References N74v N74qmentioning

confidence: 99%

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