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Title: Control of light saturated photosynthesis: Concentration and activity of ribulose bisphosphate carboxylase. Final report, September 1, 1993--February 28, 1997

Abstract

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is one of the most abundant enzymes on the planet and is responsible for catalysing the net fixation of CO{sub 2} into organic matter. It is central, therefore, to primary productivity in marine and terrestrial ecosystems. Rubisco is a large enzyme with low substrate affinity and low catalytic efficiency and is considered to limit the rate of light-saturated photosynthesis. This report summarizes research into the molecular basis of the regulation of phytoplankton photosynthesis. It describes experimental and theoretical studies of the role of Rubisco in regulating the photosynthetic rate of phytoplankton. It also describes the integration of a mechanistically based phytoplankton growth model into a description of primary productivity in the sea. This work was conducted as part of the Ocean Margins Program.

Authors:
 [1]
  1. Marine Biological Association of the United Kingdom, Plymouth (United Kingdom)
Publication Date:
Research Org.:
Marine Biological Association of the United Kingdom, Plymouth (United Kingdom)
Sponsoring Org.:
USDOE Office of Energy Research, Washington, DC (United States)
OSTI Identifier:
491409
Report Number(s):
DOE/ER/62092-T1
ON: DE97006774; TRN: 97:004202
DOE Contract Number:  
FG02-95ER62092
Resource Type:
Technical Report
Resource Relation:
Other Information: PBD: May 1997
Country of Publication:
United States
Language:
English
Subject:
14 SOLAR ENERGY; 55 BIOLOGY AND MEDICINE, BASIC STUDIES; CARBOXYLASE; ENZYME ACTIVITY; PHYTOPLANKTON; PHOTOSYNTHESIS; PROGRESS REPORT; AFFINITY; RIBULOSE; CARBON DIOXIDE FIXATION

Citation Formats

Geider, R J, and Univ. of Delaware, Lewes, DE. Control of light saturated photosynthesis: Concentration and activity of ribulose bisphosphate carboxylase. Final report, September 1, 1993--February 28, 1997. United States: N. p., 1997. Web. doi:10.2172/491409.
Geider, R J, & Univ. of Delaware, Lewes, DE. Control of light saturated photosynthesis: Concentration and activity of ribulose bisphosphate carboxylase. Final report, September 1, 1993--February 28, 1997. United States. doi:10.2172/491409.
Geider, R J, and Univ. of Delaware, Lewes, DE. Thu . "Control of light saturated photosynthesis: Concentration and activity of ribulose bisphosphate carboxylase. Final report, September 1, 1993--February 28, 1997". United States. doi:10.2172/491409. https://www.osti.gov/servlets/purl/491409.
@article{osti_491409,
title = {Control of light saturated photosynthesis: Concentration and activity of ribulose bisphosphate carboxylase. Final report, September 1, 1993--February 28, 1997},
author = {Geider, R J and Univ. of Delaware, Lewes, DE},
abstractNote = {Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is one of the most abundant enzymes on the planet and is responsible for catalysing the net fixation of CO{sub 2} into organic matter. It is central, therefore, to primary productivity in marine and terrestrial ecosystems. Rubisco is a large enzyme with low substrate affinity and low catalytic efficiency and is considered to limit the rate of light-saturated photosynthesis. This report summarizes research into the molecular basis of the regulation of phytoplankton photosynthesis. It describes experimental and theoretical studies of the role of Rubisco in regulating the photosynthetic rate of phytoplankton. It also describes the integration of a mechanistically based phytoplankton growth model into a description of primary productivity in the sea. This work was conducted as part of the Ocean Margins Program.},
doi = {10.2172/491409},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1997},
month = {5}
}