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In this study we have examined the biochemical attributes of the redox systems that regulate human sperm function using 2‐(4‐iodophenyl)‐3‐(4‐nitrophenyl)‐5‐(2,4‐disulphophenyl)‐2H‐tetrazolium, monosodium salt (WST‐1), lucigenin and luminol‐peroxidase as probes. WST‐1 was readily reduced by human spermatozoa in the presence of an intermediate electron acceptor (IEA) or NAD(P)H. The IEA‐mediated activity resembled a previously described trans‐membrane NADH oxidase in being inhibited by capsaicin, superoxide dismutase (SOD) and N‐ethyl maleimide, but differed in its sensitivity to p‐chloromercuriphenylsulphonic acid (pCMBS). The NAD(P)H‐induced WST‐1 reduction resembled the superficial oxidase described previously, in its sensitivity to pCMBS, but differed in its suppression by capsaicin. Lucigenin was reduced by human spermatozoa in a manner that could be inhibited by SOD and …