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Net-zero emissions chemical industry in a world of limited resources

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Net-zero emissions chemical industry in a world of limited resources

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Iron and steel production is responsible for 7% of global greenhouse gas emissions. Earlier literature finds that the long economic life of steel production equipment impedes decarbonization in line with climate targets. Here, we estimate the cumulative emissions from existing primary steel production equipment if operated as historically observed, based on furnace-level data of historical operating patterns. We find that the emissions commitment of current primary steel equipment is significantly smaller (21 Gt CO2eq) than previously suggested (52–65 Gt CO2eq). Consequently, we argue that future emissions from steel are driven not by long-lived capital but by the deployment pace of novel technologies and renewable energy provision, and a reduction of steel and energy demand. Without rapid progress in these aspects, the operation of current steel production equipment is likely to consume significant amounts of the remaining carbon budget. We recommend monitoring of emission-intensive asset aging and regulation of their operation.

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Integration of carbon capture with utilization technologies can lead the way to a net-zero carbon economy. Nevertheless, direct chemical conversion of chemically captured CO2 remains challenging due to its thermodynamic stability. Here, we demonstrate CO2 capture from flue gas/air and its direct conversion into syngas under solar irradiation without any externally applied voltage. The system captures CO2 with an amine/hydroxide solution and photoelectrochemically converts it into syngas (CO:H2 1:2 (concentrated CO2), 1:4 (simulated flue gas), and 1:30 (air)) using a perovskite-based photocathode with an immobilized molecular Co-phthalocyanine catalyst. At the anode, plastic-derived ethylene glycol is oxidized into glycolic acid over a Cu26Pd74 alloy catalyst. The overall process uses flue gas/air as carbon source and discarded plastic waste as electron donor, opening avenues for integrated carbon-neutral/negative solar fuel and waste upcycling technologies.

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Methane emissions along biomethane and biogas supply chains are underestimated
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Mitochondrial Targeted Cytochrome P450 2E1 (P450 MT5) Contains an Intact N Terminus and Requires Mitochondrial Specific Electron Transfer Proteins for Activity
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Hepatic mitochondria contain an inducible cytochrome P450, referred to as P450 MT5, which cross-reacts with antibodies to microsomal cytochrome P450 2E1. In the present study, we purified, partially sequenced, and determined enzymatic properties of the rat liver mitochondrial form. The mitochondrial cytochrome P450 2E1 was purified from pyrazole-induced rat livers using a combination of hydrophobic and ion-exchange chromatography. Mass spectrometry analysis of tryptic fragments of the purified protein further ascertained its identity. N-terminal sequencing of the purified protein showed that its N terminus is identical to that of the microsomal cytochrome P450 2E1. In reconstitution experiments, the mitochondrial cytochrome P450 2E1 displayed the same catalytic activity as the microsomal counterpart, although the activity of the mitochondrial enzyme was supported exclusively by adrenodoxin and adrenodoxin reductase. Mass spectrometry analysis of tryptic fragments and also immunoblot analysis of proteins with anti-serine phosphate antibody demonstrated that the mitochondrial cytochrome P450 2E1 is phosphorylated at a higher level compared with the microsomal counterpart. A different conformational state of the mitochondrial targeted cytochrome P450 2E1 (P450 MT5) is likely to be responsible for its observed preference for adrenodoxin and adrenodoxin reductase electron transfer proteins.

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