The same metal. Therefore the same creature.
Silver jams the last enzyme in the oxygen chain, in muscle packed denser with mitochondria than anything human.
Silver, second route
Vulnerability · Cytochrome c oxidasePlate · LCAN · Silver, second route · theoretical reconstruction
A mitochondrion in section. — cytochrome c oxidase — enlarged: CuA, and the haem a3–CuB pair. Silver ions occupying the copper seats. The catalytic cycle frozen. The same metal as the vampire plate. A different enzyme. Not a short circuit. A lock.
Cytochrome c oxidase — Complex IV — is the terminal enzyme of aerobic life: the site where electrons finally meet molecular oxygen. Silver ions bind the copper centres, CuA in subunit II and the haem a3-CuB binuclear site in subunit I, displace copper, and freeze the catalytic cycle at both the electron-entry point and the oxygen-reduction step. In a shifted those enzymes are running at maximum in muscle of extraordinary mitochondrial density. Local inhibition is immediately catastrophic.
Cascade propagation does the rest. The electron-transport chain backs up. Lactate surges. Oxygen-poor, acid blood hits a heart that is itself a shifted, mitochondria-dense organ. Cardiac function degrades metabolically before free silver ions ever arrive — they are scavenged by albumin and metallothionein. The wound becomes a systemic crisis because the engine is systemic. Same metal as the . Different molecular target. Convergence is evidence, not folklore recycling.
Ch. 16
Werewolves in Theory