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Life Sciences

University of Connecticut

UCHC Articles - Research

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Full-Text Articles in Physical Sciences and Mathematics

Proteo-Lipobeads For The Oriented Encapsulation Of Membrane Proteins, Leslie M. Loew Apr 2015

Proteo-Lipobeads For The Oriented Encapsulation Of Membrane Proteins, Leslie M. Loew

UCHC Articles - Research

As a surrogate of the life cell, proteo-lipobeads are presented, encapsulating functional membrane proteins in a strict orientation into a lipid bilayer. Assays can be performed just as on life cells, for example using fluorescence measurements. As a proof of concept, we have demonstrated proton transport through cytochrome c oxidase.


Coordination Of Peroxide To The Cum Center Of Peptidylglycine Α-Hydroxylating Monooxygenase (Phm): Structural And Computational Study, Betty A. Eipper, Richard E. Mains Feb 2013

Coordination Of Peroxide To The Cum Center Of Peptidylglycine Α-Hydroxylating Monooxygenase (Phm): Structural And Computational Study, Betty A. Eipper, Richard E. Mains

UCHC Articles - Research

Many bioactive peptides, such as hormones and neuropeptides, require amidation at the C terminus for their full biological activity. Peptidylglycine α-hydroxylating monooxygenase (PHM) performs the first step of the amidation reaction—the hydroxylation of peptidylglycine substrates at the Cα position of the terminal glycine. The hydroxylation reaction is copper- and O2-dependent and requires 2 equiv of exogenous reductant. The proposed mechanism suggests that O2 is reduced by two electrons, each provided by one of two nonequivalent copper sites in PHM (CuH and CuM). The characteristics of the reduced oxygen species in the PHM reaction and …