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University of Illinois at Urbana-Champaign

Localization, biochemical characterization, and solubilization of (4-vinyl) chlorophyllide a reductase, a novel chlorophyll a biosynthetic enzyme

Abstract

dc:description

(4-vinyl) chlorophyllide a reductase (4VCR), catalyses the conversion of divinyl chlorophyllide a (DVChlide a) to monovinyl chlorophyllide a (MVChlide a). The latter is the immediate precursor of monovinyl chlorophyll a (MVChl a) in plants and algae. In reaction center and light harvesting pigment-protein complexes, MVChl a is the main, photosynthetically active protein.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Plant Biology
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2011

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Parham, Ramin
Contributors dc:contributor
  • Rebeiz, Constantin A.

Subjects

dc:subject × 2

Rights

dc:rights
Statement dc:rights
  • Copyright 1994 Parham, Ramin
Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
AAI9512507
(UMI)AAI9512507
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/19130

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Parham, Ramin. Localization, biochemical characterization, and solubilization of (4-vinyl) chlorophyllide a reductase, a novel chlorophyll a biosynthetic enzyme. Dissertation thesis, University of Illinois at Urbana-Champaign, 2011. http://hdl.handle.net/2142/19130