PubMed · 5833800
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E Myhre. 1965-04-15. [Intoxication with iron tablets].. https://pubmed.ncbi.nlm.nih.gov/5833800/
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Ammonia-oxidizing archaea (AOA) are among the most abundant microorganisms in the ocean, playing a fundamental role in the marine nitrogen cycle. Although temperature and trace metal availability each individually influence the growth and activity of marine AOA, there is only a very limited understanding of the interactive effects of these two major factors on AOA in the rapidly changing ocean. Here, we show that the iron requirements of the model marine AOA species Nitrosopumilus maritimus SCM1 are highly sensitive to temperature changes. A 5 °C increase in growth temperature reduced SCM1 iron requirements by >80%, and was associated with a substantial increase in iron use efficiencies (IUE, mol C fixed/h/mol cellular Fe) under iron-limited and warming conditions. A thermally enhanced IUE enables SCM1 to more efficiently utilize scarce available iron supplies to support its growth. Whole-cell proteomic analysis revealed that iron limitation decreased expression of a ferredoxin and increased expression of a copper-dependent plastocyanin that became more pronounced with warming, suggesting coordinated electron transport response regulation under combined iron and temperature stress. The global impacts of these temperature-dependent changes to AOA iron demands were assessed using sensitivity experiments with a state-of-the-art biogeochemical model. Simulations showed that impacts on nitrification were concentrated at higher latitudes, but the alterations to ammonia concentrations were redistributed toward lower latitudes by mode and intermediate water transport. These findings reveal a previously unrecognized mechanism by which ocean warming may alleviate iron limitation of AOA, enhance their ecological competitiveness, and reshape ocean nitrogen cycling throughout marine ecosystems.
Chromochloris zofingiensis is of interest for its ability to perform a reversible trophic switch in the presence of glucose that is characterized by a shutdown of photosynthesis and an accumulation of energy storage metabolites. Previous work has shown that this trophic switch is accompanied by overflow metabolism and the production of lactate in aerobic conditions. This trophic switch is not observed in nutrient replete media. We utilized isotopically assisted metabolic flux analysis to characterize intracellular flux distributions that are associated with different metabolic phenotypes observed in this organism in different media formulations in light and dark conditions. The results of this analysis showed that low iron cultures have no flux through carbon fixation reactions, and that the carbon flux entering the TCA cycle in these cultures is approximately 40 % lower than that in iron replete cultures grown heterotrophically. This analysis was complemented with transcriptomics data collected for C. zofingiensis grown in iron limited conditions to provide further evidence towards the negative impact of iron limitation on both photosynthetic and respiratory activity. Overflow metabolism allows this alga to compensate for the lower energy production that results from iron limitation. This work highlights how nutrient availability can lead to changes in the metabolism of C. zofingiensis.
Non-heme diiron clusters occur in a number of enzymes (e.g., ribonucleotide reductase, methane monooxygenase, and Delta9-stearoyl-ACP desaturase) that activate O2 for chemically difficult oxidation reactions. In each case, a kinetically labile peroxo intermediate is believed to form when O2 reacts with the diferrous enzyme, followed by O-O bond cleavage and the formation of high-valent iron intermediates [formally Fe(IV)] that are thought to be the reactive oxidants. Greater kinetic stability of a peroxodiiron(III) intermediate in protein R2 of ribonucleotide reductase was achieved by the iron-ligand mutation Asp84 --> Glu and the surface mutation Trp48 --> Phe. Here, we present the first definitive evidence for a bridging, symmetrical peroxo adduct from vibrational spectroscopic studies of the freeze-trapped intermediate of this mutant R2. Isotope-sensitive bands are observed at 870, 499, and 458 cm-1 that are assigned to the intraligand peroxo stretching frequency and the asymmetric and symmetric Fe-O2-Fe stretching frequencies, respectively. Similar results have been obtained in the resonance Raman spectroscopic study of a peroxodiferric species of Delta9-stearoyl-ACP desaturase [Broadwater, J. A., Ai, J., Loehr, T. M., Sanders-Loehr, J., and Fox, B. G. (1998) Biochemistry 37, 14664-14671]. Similarities among these adducts and transient species detected during O2 activation by methane monooxygenase hydroxylase, ferritin, and wild-type protein R2 suggest the symmetrical peroxo adduct as a common intermediate in the diverse oxidation reactions mediated by members of this class.