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1. Geometrical analysis of cytochrome c unfolding

   https://doi.org/10.1080/00268976.2010.521202  

   Urie, Kristopher G.; Pletneva, Ekaterina; Gray, Harry B.; Winkler, Jay R.; Kozak, John J. (January 2011, Molecular Physics)
2. Nitrogen-Vacancy Magnetic Relaxometry of Nanoclustered Cytochrome C Proteins

   https://doi.org/10.1021/acs.nanolett.3c03843  

   Lamichhane, Suvechhya; Timalsina, Rupak; Schultz, Cody; Fescenko, Ilja; Ambal, Kapildeb; Liou, Sy-Hwang; Lai, Rebecca Y.; Laraoui, Abdelghani (January 2024, Nano Letters)
3. Curvature-Dependent Binding of Cytochrome c to Cardiolipin

   https://doi.org/10.1021/jacs.0c07301  

   Elmer-Dixon, Margaret M.; Xie, Ziqing; Alverson, Jeremy B.; Priestley, Nigel D.; Bowler, Bruce E. (November 2020, Journal of the American Chemical Society)

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4. Engineered Cytochrome c-Catalyzed Lactone-Carbene B–H Insertion

   https://doi.org/10.1055/s-0037-1611662  

   Chen, Kai; Huang, Xiongyi; Zhang, Shuo-Qing; Zhou, Andrew; Kan, S. B.; Hong, Xin; Arnold, Frances (February 2019, Synlett)

   Previous work has demonstrated that variants of a heme protein, Rhodothermus marinus cytochrome c (Rma cyt c), catalyze abiological carbene boron–hydrogen (B–H) bond insertion with high efficiency and selectivity. Here we investigated this carbon–boron bond-forming chemistry with cyclic, lactone-based carbenes. Using directed evolution, we obtained a Rma cyt c variant BORLAC that shows high selectivity and efficiency for B–H insertion of 5- and 6-membered lactone carbenes (up to 24,500 total turnovers and 97.1:2.9 enantiomeric ratio). The enzyme shows low activity with a 7-membered lactone carbene. Computational studies revealed a highly twisted geometry of the 7-membered lactone carbene intermediate relative to 5- and 6-membered ones. Directed evolution of cytochrome c together with computational characterization of key iron-carbene intermediates has allowed us to expand the scope of enzymatic carbene B–H insertion to produce new lactone-based organoborons. 

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5. Recurrent evolutionary switches of mitochondrial cytochrome c maturation systems in Archaeplastida

   https://doi.org/10.1038/s41467-024-45813-y  

   Li, Huang; Akella, Soujanya; Engstler, Carina; Omini, Joy J.; Rodriguez, Moira; Obata, Toshihiro; Carrie, Chris; Cerutti, Heriberto; Mower, Jeffrey P. (February 2024, Nature Communications)

   Abstract Mitochondrial cytochromecmaturation (CCM) requires heme attachment via distinct pathways termed systems I and III. The mosaic distribution of these systems in Archaeplastida raises questions about the genetic mechanisms and evolutionary forces promoting repeated evolution. Here, we show a recurrent shift from ancestral system I to the eukaryotic-specific holocytochromecsynthase (HCCS) of system III in 11 archaeplastid lineages. Archaeplastid HCCS is sufficient to rescue mutants of yeast system III and Arabidopsis system I. Algal HCCS mutants exhibit impaired growth and respiration, and altered biochemical and metabolic profiles, likely resulting from deficient CCM and reduced cytochromec-dependent respiratory activity. Our findings demonstrate that archaeplastid HCCS homologs function as system III components in the absence of system I. These results elucidate the evolutionary trajectory and functional divergence of CCM pathways in Archaeplastida, providing insight into the causes, mechanisms, and consequences of repeated cooption of an entire biological pathway. 

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