K
Kirk Cammarata
Researcher at Texas A&M University–Corpus Christi
Publications - 14
Citations - 565
Kirk Cammarata is an academic researcher from Texas A&M University–Corpus Christi. The author has contributed to research in topics: Seagrass & Light-harvesting complex. The author has an hindex of 10, co-authored 12 publications receiving 534 citations. Previous affiliations of Kirk Cammarata include University of Kentucky & University of Georgia.
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Journal ArticleDOI
Spinach Thylakoid Polyphenol Oxidase : ISOLATION, ACTIVATION, AND PROPERTIES OF THE NATIVE CHLOROPLAST ENZYME
John H. Golbeck,Kirk Cammarata +1 more
TL;DR: A large seasonal variation in polyphenol oxidase activity may result from a decrease in enzyme content rather than inhibition of the enzyme present.
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In vitro reconstitution of the photosystem I light-harvesting complex LHCI-730: heterodimerization is required for antenna pigment organization.
TL;DR: In vitro reconstitution of photosystem I light-harvesting complexes with pigments and proteins obtained by overexpression of tomato Lhca genes in Escherichia coli resembles the native LHCI-730 dimer from tomato leaves with regard to spectroscopic properties, pigment composition, and stoichiometry.
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Studies on 17,24 kD Depleted Photosystem II Membranes : I. Evidences for High and Low Affinity Calcium Sites in 17,24 kD Depleted PSII Membranes from Wheat versus Spinach
Kirk Cammarata,George M. Cheniae +1 more
TL;DR: During 17,24 kilodalton extraction by NaCl, spinach PSII is more susceptible than wheat PSII to loss of high affinity Ca and irreversible inhibition of O(2) evolution.
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In vitro reconstitution of a light-harvesting gene product: deletion mutagenesis and analyses of pigment binding.
TL;DR: AB96, a gene encoding a Pisum sativum chlorophyll a/b binding protein, can be expressed in Escherichia coli and reconstituted with pigments by the procedure described by Plumley and Schmidt and is shown to have similar pigment-binding characteristics to native CP2 complexes isolated from thylakoid membranes.
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Depletion of Photosystem II-extrinsic proteins: II. Analysis of the PS II/water-oxidizing complex by measurements of N,N,N′,N′-tetramethyl-p-phenylenediamine oxidation following an actinic flash
TL;DR: The effects of selective extractions of Photosystem II (PS II) extrinsic proteins (with and without extraction of PS II Mn) on the coupling between the PS II trap and the S-state complex were determined by analysis of steady-state O 2 evolution, chemical reactivity, and the kinetics of TMPD oxidation after a single short actinic flash.