a Exobiology Division, Ames Research Center, National Aeronautics and Space Administration, Moffett Field, California 94035
ABSTRACT
The observation that adenosine triphosphate (ATP)-dependent CO2 fixation in extracts of chemosynthetic and photosynthetic autotrophs may be regulated in part by adenosine monophosphate (AMP) was extended to the strict autotroph Thiobacillus neapolitanus (X). In addition, this report presents data which include adenosine diphosphate (ADP) in the regulatory role. When the primary CO2 acceptor, ribose-5-phosphate, was replaced by ribulose-1,5-diphosphate, no inhibition of CO2 fixation occurred unless the Mg++ concentration was limiting. A molar ratio of 5:1 AMP or ADP to ATP reduced the specific activity (micromoles of CO2 fixed per milligram of protein per minute) of the extracts from 0.22 to 0.12 and 0.11, respectively. The reported stimulation of the carboxylative phase of ATP-dependent CO2 fixation by reduced nicotinamide adenine dinucleotide (NADH2) was investigated. Adding NADH2 to the extracts did not stimulate CO2 fixation, even at carbonate levels from 0.05 to 30 µmoles, except in the absence of ribose-5-phosphate. Slight increases in CO2 fixation were noted when the assay system was incubated in air instead of the usual helium atmosphere.
2 National Academy of SciencesNational Research Council Postdoctoral Resident Research Associate at Ames Research Center. Present address: Department of Microbiology, Colorado State University, Fort Collins 80521.
3 Present address: Bruce Lyon Memorial Research Laboratory, Oakland, Calif.
1 Presented in part at the 66th Annual Meeting of The American Society for Microbiology, Los Angeles, Calif., 1966.
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| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
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