{'fraction_non_alphanumeric': 0.02147766323024055, 'fraction_numerical': 0.0, 'mean_word_length': 5.43646408839779, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Redox (In)activations of Metalloenzymes: A Protein Film Voltammetry Approach

Redox metalloenzymes are omnipresent in living organisms where they catalyze key cellular reactions with great e ﬃ ciency. These enzymes can often be reversibly placed into inactive states following changes in redox conditions. This is a hindrance for their use in biotechnological devices, and also a complication for their study via a structure / function approach, because structural data alone usually is not enough to discriminate between active and inactive states. However, these inactive states can also inform on the chemistry of the enzyme’s active sites and on their catalytic cycles. A technique that has proved particularly valuable in the last decades for studying these processes is Protein Film Voltammetry (PFV), in which an enzyme is immobilized on an electrode in a conﬁguration where direct electron transfer is possible. In this article, we review the studies of redox (in)activation processes using PFV, present the theory for a number of cases (reversible inactivations, irreversible activations), and give guidelines to obtain and intepret suitable kinetic data.