Sriram Satagopan

ORCID: 0000-0002-4867-531X
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About
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Algal biology and biofuel production
  • Microbial Metabolism and Applications
  • Advanced Thermodynamics and Statistical Mechanics
  • Microbial Community Ecology and Physiology
  • Microbial Metabolic Engineering and Bioproduction
  • Microbial metabolism and enzyme function
  • Porphyrin Metabolism and Disorders
  • Catalysis and Oxidation Reactions
  • Genomics and Phylogenetic Studies
  • CO2 Sequestration and Geologic Interactions
  • Carbon Dioxide Capture Technologies
  • Photoreceptor and optogenetics research
  • Enzyme Structure and Function
  • Plant biochemistry and biosynthesis
  • Metal Extraction and Bioleaching
  • Mitochondrial Function and Pathology
  • Metal-Catalyzed Oxygenation Mechanisms
  • Biotin and Related Studies
  • Amino Acid Enzymes and Metabolism
  • Enzyme Catalysis and Immobilization
  • Plant-Derived Bioactive Compounds
  • Metalloenzymes and iron-sulfur proteins
  • Microbial Natural Products and Biosynthesis
  • CO2 Reduction Techniques and Catalysts

American Chemical Society
2022-2023

The Ohio State University
2007-2020

University of Nebraska–Lincoln
2004-2008

DuPont (United States)
2008

Swedish University of Agricultural Sciences
2007

Island Hospital
2005

Louisiana State University Health Sciences Center New Orleans
2005

Metagenomic studies recently uncovered form II/III RubisCO genes, originally thought to only occur in archaea, from uncultivated bacteria of the candidate phyla radiation (CPR). There are no isolated CPR and these organisms predicted have limited metabolic capacities. Here we expand known diversity lineages. We report a RubisCO, distantly similar archaeal III some Parcubacteria (OD1), WS6 Microgenomates (OP11) phyla. In addition, significantly Peregrinibacteria (PER) first sequences To...

10.1038/ismej.2016.53 article EN cc-by-nc-sa The ISME Journal 2016-05-03

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the rate-limiting step of photosynthetic CO 2 fixation and, thus, limits agricultural productivity. However, Rubisco enzymes from different species have catalytic constants. If structural basis for such differences were known, a rationale could be developed genetically engineering an improved enzyme. Residues at bottom large-subunit α/β-barrel active site green alga Chlamydomonas reinhardtii (methyl-Cys-256, Lys-258, and...

10.1073/pnas.0508042102 article EN Proceedings of the National Academy of Sciences 2005-11-10

Recapturing atmospheric CO 2 is key to reducing global warming and increasing biological carbon availability. Ralstonia eutropha a biotechnologically useful aerobic bacterium that uses the Calvin–Benson–Bassham ( CBB ) cycle enzyme ribulose 1,5‐bisphosphate carboxylase/oxygenase (Rubis for utilization, suggesting it may be host bioselect Rubis molecules with improved ‐capture capabilities. A strain of R. was constructed this purpose after deleting endogenous genes encoding two related s....

10.1111/febs.13774 article EN publisher-specific-oa FEBS Journal 2016-06-04

With increasing concerns over global warming and depletion of fossil-fuel reserves, it is attractive to develop innovative strategies assimilate CO2, a greenhouse gas, into usable organic carbon. Cell-free systems can be designed operate as catalytic platforms with enzymes that offer exceptional selectivity efficiency, without the need support ancillary reactions metabolic pathways operating in intact cells. Such are yet exploited for applications involving CO2 utilization subsequent...

10.1186/s13068-017-0861-6 article EN cc-by Biotechnology for Biofuels 2017-07-06

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) is a critical yet severely inefficient enzyme that catalyses the fixation of virtually all carbon found on Earth. Here, we report functional metagenomic selection recovers physiologically active RubisCO molecules directly from uncultivated and largely unknown members natural microbial communities. Selection based CO2 -dependent growth in host strain capable expressing environmental deoxyribonucleic acid (DNA), precluding need for pure...

10.1111/1462-2920.13138 article EN Environmental Microbiology 2015-11-30

Summary RubisCO, the CO 2 fixing enzyme of Calvin–Benson–Bassham (CBB) cycle, is responsible for majority carbon fixation on Earth. RubisCO fixes 12 faster than 13 resulting in C‐depleted biomass, enabling use δ C values to trace CBB activity contemporary and ancient environments. Enzymatic fractionation expressed as an ε value, routinely used modelling, example, global cycle climate change, interpreting trophic interactions. Although spinach ( = ~29‰) have been such efforts, there are five...

10.1111/1462-2920.14423 article EN publisher-specific-oa Environmental Microbiology 2018-09-24

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) is a ubiquitous enzyme that catalyzes the conversion of atmospheric CO2 into organic carbon in primary producers. All naturally occurring RubisCOs have low catalytic turnover rates and are inhibited by oxygen. Evolutionary adaptations its host organisms to changing oxygen concentrations provide an impetus artificially evolve RubisCO variants under unnatural selective conditions. A deletion strain nonsulfur purple photosynthetic...

10.1128/mbio.01537-19 article EN cc-by mBio 2019-07-22

Ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) is a globally significant biocatalyst that facilitates the removal and sequestration of CO2 from biosphere. Rubisco-catalyzed reduction thus provides virtually all organic carbon utilized by living organisms. Despite catalyzing rate-limiting step photosynthetic chemoautotrophic assimilation, Rubisco markedly inefficient as competition between O2 for same substrate limits ability aerobic organisms to obtain maximum amounts...

10.1021/bi9006385 article EN Biochemistry 2009-08-25

The loop between α-helix 6 and β-strand in the α/β-barrel of ribulose-1,5-bisphosphate carboxylase/oxygenase plays a key role discriminating CO2 O2. Genetic screening Chlamydomonas reinhardtii previously identified loop-6 V331A substitution that decreases carboxylation CO2/O2 specificity. Revertant selection T342I G344S substitutions restore photosynthetic growth by increasing specificity enzyme. In numerous X-ray crystal structures, is closed or open depending on activation state enzyme...

10.1021/bi701063f article EN Biochemistry 2007-09-08

Ribulose-1,5-bisphosphate is the rate-limiting enzyme in photosynthesis. The catalytic large subunit of green-algal from Chlamydomonas reinhardtii approxiamtely 90% identical to flowering-plant sequences, although they confer diverse kinetic properties. To identify regions that may account for species variation properties, directed mutagenesis and chloroplast transformation were used create four amino-acid substitutions carboxy terminus mimic sequence higher-specificity plant enzymes.The...

10.1186/1471-2229-8-85 article EN cc-by BMC Plant Biology 2008-01-01

Proximal Cys(172) and Cys(192) in the large subunit of photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae higher plants. Mutation has been shown to affect redox properties vitro delay degradation vivo under stress conditions. Here, we report effect replacement by serine on catalytic properties, thermostability three-dimensional structure Chlamydomonas reinhardtii Rubisco. The most striking C172S...

10.1042/bj20071422 article EN Biochemical Journal 2008-03-27

In the Calvin cycle of photosynthesis, ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) catalyzes conversion ribulose 1,5-bisphosphate to 3-phosphoglyceric acid (3-PGA) while incorporating atmospheric CO2 into an organic molecule. Thus, RubisCO is nature's CO2-sequestering enzyme that present in chloroplasts. As effort mitigate climate change, biomimetic carbon fixation technologies have been developed through immobilization nanostructures form nanostructure–RubisCO complexes. The...

10.1021/acssuschemeng.0c05498 article EN ACS Sustainable Chemistry & Engineering 2020-11-06

Enzymes have evolved over hundreds of years through changes in ecosystems (climate, atmosphere, hydrology, etc). The evolutionary driven by the need to survive has led enzymes with diverse functionality such as reduction carbon dioxide and methane other forms carbon, fixation nitrogen, high temperature biochemical processes. While these useful properties, engineering a scalable cell-free system will be for stable production desired products without involving vagaries cellular metabolism....

10.1088/0964-1726/25/12/125033 article EN Smart Materials and Structures 2016-11-14

The enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and its central role in capturing atmospheric CO2 via the Calvin–Benson–Bassham (CBB) cycle have been well-studied. Previously, a form II RuBisCO from Rhodopseudomonas palustris, facultative anaerobic bacterium, was shown to assemble into hexameric holoenzyme. Unlike previous studies with RuBisCO, R. palustris could be crystallized presence of transition state analogue 2-carboxyarabinitol (CABP), greatly facilitating...

10.1021/acs.biochem.9b00617 article EN Biochemistry 2019-08-28

Technological and medical advances over the past few decades epitomize human capabilities. However, increased life expectancies concomitant land-use changes have significantly contributed to release of ~830 gigatons CO2 into atmosphere last three decades, an amount comparable prior two a half centuries emissions. The United Nations has adopted pledge achieve “net zero”, i.e., yearly removing as much from emitted due activities, by year 2050. Attaining this goal will require concerted effort...

10.26434/chemrxiv-2022-j39b0 preprint EN cc-by 2022-03-24
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