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=== As an enzyme for catalytic activity === Cytochrome C has also been widely studied as an enzyme with peroxidase-like activity. Cytochrome C was conjugated to charged polymer to test its peroxidase-like activity.<ref>{{Cite journal |vauthors=Zhang Y, Wang Q, Hess H |date=March 2017 |title=Increasing enzyme cascade throughput by pH-engineering the microenvironment of individual enzymes. |journal=ACS Catalysis |volume=7 |issue=3 |pages=2047-2051 |doi=10.1021/acscatal.7b01766}}</ref><ref name="Benson_2019">{{Cite journal |vauthors=Benson KR, Gorecki J, Nikiforov A, Tsui W, Kasi RM, Kumar CV |date=April 2019 |title=Cytochrome c-poly(acrylic acid) conjugates with improved peroxidase turnover number |journal=Organic & Biomolecular Chemistry |volume=17 |issue=16 |pages=4043β4048 |doi=10.1039/c9ob00541b |pmid=30950479}}</ref> Inspired from natural examples of enzyme encapsulation in protein-based cage structures (Example: Carboxysomes, Ferritin, and Encapsulin), Cytochrome C was encapsulated in a 9 nm small self-assembling DNA binding protein from nutrient starved cells (Dps) protein cage using chimeric self-assembly approach. Authors observed unique catalytic activity behavior upon encapsulating enzyme inside a protein-cage, which was different from enzyme in solution. This was attributed to local microenvironment provided by Dps nanocage's interior cavity which is different than bulk.<ref>{{Cite journal |vauthors=Waghwani HK, Douglas, T |date=March 2021 |title=Cytochrome C with peroxidase-like activity encapsulated inside the small DPS protein nanocage |journal=Journal of Materials Chemistry B |volume=9 |issue=14 |pages=3168β3179 |doi=10.1039/d1tb00234a |pmid=33885621 |doi-access=free}}</ref>
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