Biochemistry explores the intricate chemical processes that power life, bridging the gap between biology and chemistry to explain how molecules like proteins and DNA function within living cells. This field reveals the molecular machinery behind everything from metabolism to genetic inheritance, turning complex biological mysteries into understandable chemical interactions.

On Gist.Science, we bring you the freshest discoveries in this dynamic area directly from bioRxiv. Our team processes every new preprint uploaded to the server, transforming dense academic findings into both clear, plain-language overviews and detailed technical summaries. This dual approach ensures that whether you are a curious beginner or a seasoned researcher, you can grasp the significance of these breakthroughs immediately.

Below are the latest papers in biochemistry, complete with our curated summaries to help you navigate the cutting edge of molecular science.

⚗️ biochemistry

Mechanism of GPR84 allosteric modulation at a helix 8-proximate site

This study elucidates the structural mechanism of Gi-biased allosteric modulation in the GPR84 receptor by identifying a novel helix 8-proximate binding site for the positive allosteric modulator PSB-16671, which stabilizes a specific receptor conformation to enhance macrophage phagocytosis while avoiding desensitization.

Zhang, X., Guseinov, A.-A., Jenkins, L., Zhou, J., Gossen, F., Wang, P., Al Mahmud, Z., Li, Y., Mahardhika, A. B., Mulle (…)2026-04-12
⚗️ biochemistry

Comprehensive study on ferredoxin isoforms in the cyanobacterium Synechocystis sp. PCC 6803

This study comprehensively characterizes twelve ferredoxin isoforms in *Synechocystis* sp. PCC 6803 through spectroscopic, electrochemical, and expression analyses, revealing a diverse suite of proteins with varying redox potentials and regulatory patterns that collectively maintain cellular redox homeostasis by supporting both core photosynthetic electron transfer and specialized metabolic functions.

Boehm, M., Svedruzic, D., Lubner, C. L., Appel, J., Mulder, D. W., Kisgeropoulos, E., Hueren, V., Spengler, K., Bharadwa (…)2026-04-10
⚗️ biochemistry

Isoprenoid quinone profiling in complex biological samples using a novel semi-quantitative HPLC-MS/MS method

This study introduces a novel, rapid, and sensitive semi-quantitative HPLC-MS/MS method capable of detecting the widest range of isoprenoid quinones to date, successfully revealing stage-specific microbial community shifts in wastewater treatment samples.

Roger-Margueritat, M., Reveillard, A., Filimon, A. O., Boumendjel, A., Wendisch, V. F., Plazy, C., Cunin, V., Abby, S. S (…)2026-04-10
⚗️ biochemistry

Discovery of dihydroxy-enone-type protein-bound ceramides as the dominant type in human stratum corneum

This study reveals that dihydroxy-enone-type protein-bound ceramides, rather than the previously studied epoxy-enone types, are the predominant class in human stratum corneum and are likely generated via epoxide hydrolase EPHX3-mediated conversion, highlighting a fundamental structural difference between human and mouse skin barrier lipids.

Kojima, A., Sugiyama, T., Ohno, Y., Kihara, A.2026-04-10
⚗️ biochemistry

Mapping Evidence Gap Between NMN and NR for Metabolic Outcomes: A Systematic Review, Transitivity Assessment, and Indirect Comparison Meta-Analysis

This systematic review and indirect comparison meta-analysis concludes that current evidence is structurally insufficient to reliably compare the metabolic effects of NMN and NR due to systematic asymmetries in dosing, population demographics, and assay methods, necessitating future head-to-head trials with harmonized protocols to generate interpretable comparative data.

Nguyen, A. T., Nguyen, B.2026-04-09
⚗️ biochemistry

Time-resolved cryo-EM reveals conformational trajectory of allosteric activation in isocitrate lyase

Time-resolved cryo-EM studies of *Mycobacterium tuberculosis* isocitrate lyase 2 reveal that acetyl-CoA binding drives asymmetric, half-of-site activation through a conformational selection mechanism that shifts the enzyme's pre-existing equilibrium toward an active state.

Taka, J., Jung, J., Guo, S., Jiao, W., Kwai, B. X., de Carvalho, L., McNeil, M., Huang, E. Y., Yu, Z., Leung, I. K. H. (…)2026-04-09